Mushroom lectins: Current status and future perspectives

Ram Sarup Singh; Ranjeeta Bhari; Hemant Preet Kaur

The mushroom Agaricus bisporus secretes biologically active compounds and proteins with benefits for human health. Most reported proteins from A. bisporus are tyrosinases and lectins. Lectins are of therapeutic or pharmaceutical interest. To date, only limited information is available on A. bisporus lectins and lectin-like proteins. No therapeutic products derived from A. bisporus lectin (ABL) are available on the market despite its extensive exploration. Recently, A. bisporus mannose-binding protein (Abmb) was discovered. Its discovery enriches the information and increases the interest in proteins with therapeutic potential from this mushroom. Furthermore, the A. bisporus genome reveals the possible occurrence of other lectins in this mushroom that may also have therapeutic potential. Most of these putative lectins belong to the same lectin groups as ABL and Abmb. Their relationship is discussed. Particular attention is addressed to ABL and Abmb, which have been explored for their...

A lectin was isolated from the fruiting bodies of Pholiota aurivella by preparative PAGE and named PAA (Pholiota aurivella agglutinin). PAA was a polymeric protein of more than several hundred kDa consisting of 18-kDa subunits. The amino acids were sequenced from the N-terminus of the lectin; they were YSVTTPNSVKGGTNQG. PAA agglutinated human erythrocytes regardless of blood type equally and Pronase treatment of erythrocytes increased the sensitivity to agglutination by the lectin. In a hemaggluting inhibition assay, none of the mono-and oligosaccharides used affected agglutination by the lectin. Among glycoproteins, asialofetuin was the best inhibitor. This is first isolated and characterized lectin from the family Strophariaceae.

A lectin (LEL) was isolated from the fresh fruiting bodies of the shiitake mushroom Lentinula edodes by a combination of gel filtration chromatography on Sephadex G-150 and affinity chromatography on an N-acetyl-D-galactosamine-Sepharose 4B column. Its molecular mass, as determined by gel filtration, was estimated to be 71, 000 Daltons and its structure is homotetrameric with subunit molecular weight of approximately 18,000 Daltons. LEL agglutinated non-specifically red blood cells from the human ABO system as well as rabbit erythrocytes and in hae-magglutination inhibition assays, exhibited sugar-binding specificity toward N-acetyl-D-galactosamine. EDTA had no inhibitory effect on its haemagglutinating activity, which was stable up to 70°C and was not affected by changes in pH. The lectin had no covalently-linked carbohydrate and amino acid composition analysis revealed that it contained 124 amino acid residues and was rich in tyrosine, proline, phenylalanine, arginine, glutamic acid and cysteine. LEL did not cause mortality neither was it observed to alter the morphology of key organs when administered intraperito-neally at concentrations up to 10,000 mg kg-1 body weight of mice. Keywords: Lectin, lentinula edodes, N-acetyl-D-galactosamine, shiitake mushroom, fruiting bodies, agglutination

Critical Reviews in Biotechnology, 2010; 30(2): 99–126 REVIEW ARTICLE Mushroom lectins: Current status and future perspectives Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Carbohydrate and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala, Punjab, India Abstract Lectins are nonimmune proteins or glycoproteins that bind speciically to cell surface carbohydrates, culminating in cell agglutination. These are known to play key roles in host defense system and also in metastasis. Many new sources have been explored for the occurrence of lectins during the last few years. Numerous novel lectins with unique speciicities and exploitable properties have been discovered. Mushrooms have attracted a number of researchers in food and pharmaceuticals. Many species have long been used in traditional Chinese medicines or functional foods in Japan and other Asian countries. A number of bioactive constituents have been isolated from mushrooms including polysaccharides, polysaccharopeptides, polysaccharide–protein complexes, proteases, ribonucleases, ribosome inactivating proteins, antifungal proteins, immunomodulatory proteins, enzymes, lectins, etc. Mushroom lectins are endowed with mitogenic, antiproliferative, antitumor, antiviral, and immunestimulating potential. In this review, an attempt has been made to collate the information on mushroom lectins, their blood group and sugar speciicities, with an emphasis on their biomedical potential and future perspectives. Keywords: Higher fungi; agglutinins; sugar speciicity; mitogenic potential; antiproliferative activity; immunomodulation Introduction Lectins are univalent or polyvalent proteins of nonimmune origin that bind reversibly and noncovalently to speciic sugars on the apposing cells, thus precipitating polysaccharides, glycoproteins and glycolipids bearing speciic sugars (Goldstein et al., 1980; Singh, Tiwary, and Kennedy, 1999). Owing to their speciicity to bind carbohydrates, they are capable of agglutinating erythrocytes, making their detection easy (Sharon and Lis, 1972). hese are undoubtedly the most versatile group of proteins used in biological and biomedical research. he irst lectin (then called hemagglutinin) was reported in seeds of Ricinus communis by Stillmark (1888). Since then, new lectins with interesting properties are continuously being added to the list. Lectins have been isolated and characterized from diverse sources, including plant seeds and roots, fungi, bacteria, algae, body luid of invertebrates, lower vertebrates, and mammalian cell membranes (Singh, Tiwary, and Kennedy, 1999) and have been attributed varied roles in diferent organisms. Legume lectins are involved in symbiotic association with nitrogen ixing bacteria (Brock and Madigan, 1991), while seed lectins primarily play a role in defense against insects and fungi (Mirelman et al., 1975; Janzen, Juster, and Liener, 1976; Gatehouse et al., 1995). hey can serve as reserve substances or in some cases regulate the carbohydrate metabolism or act as intermediates in the action of hormones (Grifaut, Guiltat, and Guillot, 1990). D-mannose and N-acetyl-D-glucosamine speciic macrophage lectins mediate phagocytotic events (lectinophagocytosis) of microbes such as Aspergillus fumigatus (Kan and Bennett, 1988), Klebsiella pneumoniae (Athamna, 1989a,b), Pseudomonas aeruginosa (Speert et al., 1988) and Leishmania donovani (Blackwell et al., 1985). Cell surface lectins have been known to mediate recognition processes in normal and pathological states of living organisms (Sharon and Lis, 1989). heir role in normal and tumor cell adhesion, developmental processes, lymphocyte homing, cell diferentiation, and drug targeting has been extensively reviewed (Singh, Tiwary, and Kennedy, 1999; Tiwary and Singh, 1999). he discovery of fungal lectins began with investigations on toxicology of higher fungi. he irst fungal lectin was reported in ly agaric by Ford (1910), where lectin activity was found to be associated with the toxicity of the fungi. Address for Correspondence: Ram Sarup Singh, Carbohydrate and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala 147 002, Punjab, India. E-mail: rssingh11@lycos.mail (Accepted 25 August 2009) ISSN 0738-8551 print/ISSN 1549-7801 online © 2010 Informa UK Ltd DOI: 10.3109/07388550903365048 http://www.informahealthcare.com/bty Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. 100 Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur Later reports on lectins in edible fungi such as Boletus edulis (Friedberger and Brossa, 1912) and Lactarius deliciosus (Guillot et al., 1991) evidenced the independence of toxicity and lectin activity. Lectin activities have also been reported in lower fungi including Rhizoctonia solani (Vranken et al., 1987; Candy et al., 2001), Arthrobotrys oligospora (Rosen et al., 1992), Sclerotium rolfsii (Wu et al., 2001), Sclerotinia sclerotiorum (Candy et al., 2003), Penicillium spp. (Hamilton et al., 1998; Singh et al., 2009a), Aspergillus spp. (Tronchin et al., 2002; Matsumura et al., 2007; Singh, Tiwary, and Bhari, 2008; Singh, hakur, and Bhari, 2009b), Macrophomia phaseolina (Bhowal, Guha, and Chatterjee, 2005) and Fusarium solani (Khan, Ahmad, and Khan, 2007). In fungi, they have been known to play a role in parasitism involving plants (Hohl and Balsiger, 1986), insects (Ishikawa, Oishi, and Aida, 1983) or predation to soil nematodes (Rosenzweig and Ackroyd, 1983). Speciic interactions in lichens (Lockhart, Rowell, and Stewart, 1978; Petit, 1978; Petit, Lallemant, and Savoye, 1983) have been postulated to be mediated by fungal lectins, which recognize the glycosides present on the walls of cyanobacterial partners. Lectin activity has been detected in thalli of lichen-forming basidiomycete Dictyonema glabratum (Eliio et al., 2000). Fungal lectins have been also known to intervene with the early stages of ectomycorrhizal symbiosis (Guillot et al., 1994). Lectin from carpophores of Lactarius deterrimus has been demonstrated to play a role in recognition in the early stages of mycorrhizae formation with Picea abies (Giollant et al., 1993). Mushrooms elaborate high levels of lectins, suggesting their existence as a kind of storage protein as in plants. Toxicity of lectins from Volvariella volvacea and Agrocybe aegerita in mice and antiviral activity of many mushroom lectins provide evidence of their possible role in defense such as plant lectins. Certain lectins are stage-speciic and promote mycelial diferentiation to fruiting bodies as in Flammulina velutipes (Tsuda, 1979; Yatohgo et al., 1988), Coprinus cinereus (Cooper et al., 1997) and A. aegerita (Sun et al., 2003). Lectin activity of Pleurotus ostreatus fruiting bodies has been reported to be closely associated with α-galactosidase activity (Conrad and Rudiger, 1994) and is known to activate endogenous phosphatase (Brechtel, Wätzig, and Rüdiger, 2001). Mushrooms have been long known for their nutritive and medicinal values and now represent a rich source of lectins. here is an ever increasing interest in mushroom lectins due to their unique carbohydrate-binding speciicities. Lectins from higher fungi have been extensively reviewed by Guillot and Konska (1997) and Wang, Ng, and Liu (1998a). he comparison of structures of mushroom lectins whose crystal structure is known, has been reviewed recently (Goldstein and Winter, 2007). his review focuses mainly on the occurrence of lectins within mushrooms, their characteristics, and therapeutic potential. Actinomycetes (Ogawa et al., 2001; Otta et al., 2002; Liu, Wang, and Ng, 2006; Jung et al., 2007; Wong, Wang, and Ng, 2009). Distribution of lectins amongst Basidiomycetes is given in Figure 1. Amongst them, lectin activity is usually present in the fruiting bodies with a few exceptions of mycelial lectins. Extracellular lectin activity is reported in shiitake mushroom Lentinus edodes growing in submerged cultures (Tsivileva, Nikitina, and Garibova, 2005). he same organism also expresses intracellular lectin activity in mycelia (Vetchinkina et al., 2008a) and fruiting bodies which does not interact strongly with carbohydrates (Wang, Ng, and Ooi, 1999). Aleuria aurantia is known to express lectin activity in vegetative mycelium as well as fruiting bodies (Kochibe and Furukawa, 1980; Kochibe and Matta, 1989; Ogawa et al., 1998). Mycelial lectins have also been reported in A. aegerita (Ticha et al., 1985), Kuehneromyces mutabilis, Pholiota squarrosa (Musilek et al., 1990), and Ganoderma lucidum (Kawagishi et al., 1997). Two kinds of lectins have been reported in Pleurotus cornucopiae synthesized at speciic developmental stages, one in fruiting bodies and the other in mycelial aggregates (Kaneko et al., 1993; Yoshida et al., 1994; Oguri et al., 1996; Iijima et al., 2003). Tricholoma mongolicum is known to express diferent lectins in mycelia (Wang et al., 1995) and fruiting bodies (Wang, Ng, and Ooi, 1998b). Lectin activity has been documented in fruiting bodies (Kawagishi et al., 1990) and mycelia (Stepanova et al., 2006; Stepanova, Nikitina, and Boiko, 2007) of Grifola frondosa, the latter being difusely distributed on the surface of hyphae (Stepanova et al., 2009). Mikiashvili and co-authors (2006) in an extensive study have compared the lectin activities of extracts from fruiting bodies and mycelia of medicinal and edible basidiomycete mushrooms and found lectin activities in extracts of fruiting bodies of Agaricus pilatianus, Coprinus comatus, C. micaceus, Macrolepiota rachodes, Tricholoma fractum, Amanita ovoidea, Melanoleuca brevipes, Leucoagaricus leucothitus and Lepista nuda, and mycelial extracts of Cerrena unicolor, Ganoderma ramnosissmum, Ganoderma lucidum, and Trametes versicolor. Mushrooms known to produce lectins are summarized in Table 1. he occurrence of lectins in higher fungi is wider than in higher plants and they express higher levels of lectins; 10% 61% 15% 9% Agaricales An overview of mushroom lectins Many Basidiomycetes have been reported for lectin activity, but there are a fewer reports on lectin activity from 5% Polyporales Russulales Boletales Others* * Thelephorales: 0.96%; Auriculariales: 0.33%; Cantharellales: 0.64%; Hymenochaetales: 1.6%; Gomphales: 0.33%; Lycoperdales: 0.96%. Figure 1. Distribution of lectins amongst Basidiomycetes. Mushroom lectins Table 1. Localization of lectins in mushrooms. Source Common namea Agaricus abruptibulbus Abruptly-bulbous agaricus Agaricus arvensis Horse mushroom Agaricus bisporus Button mushroom Agrocybe aegerita Royal Sun agaricus Field mushroom/Meadow mushroom n.s. Wood mushroom Blushing wood mushroom/Red staining mushroom/ Bleeding mushroom Black poplar mushroom F&M Agrocybe cylindracea Agrocybe erebia Aleuria aurantia Toadstool Dark ieldcap Orange peel mushroom F F F&M Amanita citrina Amanita crocea Amanita excelsa Amanita fulva Amanita muscaria Amanita ovoidea Amanita phalloides False death cap/Citron amanita Orange grisette Grey spotted amanita Tawny grisette/Orange-brown ringless amanita Fly agaric n.s. Death cap F F F F F F F Amanita porphyria Amanita pseudoporphyria Amanita spissacea Amanita strobiliformis Amanita vaginata Amantia pantherina Armillaria luteo-virens Armillaria mellea Ascoclavulina sakaii Ascocoryne cylichnium Auricularia polytricha Bjerkandera adusta Bolbitius vitellinus Boletopsis leucomelas Boletus aestivalis Boletus badius Boletus edulis Boletus erythropus Boletus parasitsicus Boletus pinicola Boletus piperatus Boletus pruinatus Boletus satanus Boletus subtomentosus Calvatia caelata Calvatia craniiformis Cantharellus cibarius Cerrena unicolor Chlorophyllum molybdites Ciborinia camelliae Clavaria fumosa Clavaria vermicularis Clavicorona pyxidata Grey veiled amanita Hongo’s false death cap n.s. European pine/Cone lepidella White ringless amanita/Grisette Panther Golden mushroom Honey mushroom n.s. n.s. Tree ear/Cloud ear Smoky polypore Yellow cow-pat toadstool/Yellow ieldcap Black falsebolete/Kurokawa Summer cep Bay bolete King bolete/Penny bun Dotted stem bolete n.s. Pine bolete/Spring king Peppery bolete n.s. Devil’s bolete Yellow-cracked boletus Pufball mushroom Pufball mushroom Chantarelle/Chanterelle Mossy maze polypore Green-spored parasol/Green gill Flower blight/Petal blight Grayish fairy club White worm coral/Fairy ingers Crown-tipped coral F F F F F F F F F F F F F F F F F F F F F F F F F F F M F F F F F Agaricus blazei Agaricus campestris Agaricus pilatianus Agaricus silvicola Agaricus sylvaticus Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Location of lectin F F F F F F F F 101 Reference(s) Yagi et al. (2000) Pemberton (1994) Sage and Connett, (1969); Sueyoshi, Tsuji, and Osawa (1985) Kawagishi et al. (1988) Sage and Vazquez (1967) Mikiashvili et al. (2006) Pemberton (1994) Pemberton (1994) Zhao et al. (2003); Guillot and Konska (1997) Wang et al. (2002a); Yagi et al. (1997) Pemberton (1994) Kochibe and Furukawa (1980); Ogawa et al. (1998) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Mikiashvili et al. (2006) Lutsik-Kordovsky, Stasyk, and Stoika (2001) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Zhuang et al. (1996) Feng et al. (2006) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Yagi and Tadera (1988) Pemberton (1994) Pemberton (1994) Koyama et al. (2002) Pemberton (1994) Pemberton (1994) Zheng et al. (2007) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton 1994 Zheng et al. (2007) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Mikiashvili et al. (2006) Kobayashi et al. (2004) Otta et al. (2002) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Table 1. continued on next page 102 Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Table 1. Continued. Source Clavulina cinerea Clavulinopsis corniculata Clavulinopsis fusiformis Clavulinopsis helvola Clitocybe clavipes Clitocybe laccida Clitocybe fragrans Clitocybe geotropa Clitocybe gibba Clitocybe langei Clitocybe nebularis Clitocybe obsoleta Clitocybe rivulosa Collybia acervata Collybia butyracea Collybia cirrhata Collybia conluens Collybia dryophila Collybia fusipes Coltricia cinnamomea Coltricia perennis Conocybe blattaria Coprinus acuminatus Coprinus atramentarius Coprinus cinereus Coprinus comatus Common namea Ashy coral mushroom Meadow coral Spindle-shaped yellow coral Yellow club Club-footed clitocybe Tawny funnel Cap Fragrant funnel Trooping funnel Common funnel cap n.s. Clouded funnel n.s. Fool’s funnel n.s. Greasy tough-shank/Butter cap Piggyback shanklet Mushroom clustered toughshank n.s. Spindle toughshank Shiny cinnamon polypore Tiger’s eye n.s. Humpback inkcap n.s. Shaggy dung coprinus Shaggy inkcap/Lawyer’s wig Coprinus lagopus Coprinus micaceus Hare’s foot inkcap Mica cap Coprinus plicatilis Cordyceps militaris Coriolus hirsutus Coriolus versicolor Cortinarius anomalus Cortinarius balteatus Cortinarius salor Crepidotus mollis Crepidotus variabilis Crinipellis stipitaria Cryptoporus volvatus Cyathus stercoreus Dacrymyces palmatus Daedalea dickinsii Daedaleopsis confragosa Daedaleopsis tricolor Descolea lavoannulata Elfvingia applanata Entoloma porphyrophaeum Entoloma rhodopolium Entoloma sericatum Entoloma staurosporum Flammulina velutipes Fomes fomentarius Pleated inkcap Scarlet caterpillar club n.s. Polypore versicolor Variable webcap n.s. Violet cort Jelly crep Variable oysterling n.s. Veiled polypore Dung loving bird’s nest Witch’s butter n.s. hin-maze lat polypore Blushing bracket n.s. n.s. Lilac pinkgill Midnight blue entoloma n.s. n.s. Velvet foot Touchwood fungus/True tinder Polypore/Hoof fungus n.s. n.s. Fomitella fraxinea Funalia trogii Location of lectin F F F F F F F F F F F F F F F F F F F F F F F M F F M F F F F F F F F F F F F F F F F F F F F F F F F F&M F M Reference(s) Pemberton (1994) Pemberton (1994) Furukawa et al. (1995) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994); Yagi et al. (2000) Pemberton (1994) Horejsi and Kocourek (1978) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Pemberton (1994) Banerjee et al. (1982) Cooper et al. (1997) Pemberton (1994); Mikiashvili et al. (2006) Banerjee et al. (1982) Yagi et al. (2000); Mikiashvili et al. (2006) Pemberton (1994) Jung et al. (2007) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Yatohgo et al. (1988) Pemberton (1994); Pardoe et al. (1969); Devitashvili et al. (2008) Kim et al. (2007) Devitashvili et al. (2008) Table 1. continued on next page Mushroom lectins 103 Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Table 1. Continued. Source Galerina fasciculata Ganoderma adspersum Ganoderma applanatum Ganoderma capense Ganoderma ramnosissmum Ganoderma lucidum Common namea n.s. n.s. Artist’s conk n.s. n.s. Reishi mushroom/Ling zhi Location of lectin F F M F M F&M Geoglossum cookeanum Grifola frondosa n.s. Hen of the woods/Maitake F F&M Gymnopilus chrysimyces Gymnopilus liquiritiae Gymnopilus spectabilis Gyroporus castaneus Helvella acetabulum Helvella atra Helvella crispa Helvella elastica Helvella lacunosa Hericium erinaceum Hohenbuehelia serotina Hydnum repandum Hygrocybe coccinea Hygrocybe lavescens Hygrophoropsis aurantiaca Hygrophorus caprealarius Hygrophorus chlorophanus Hygrophorus coccineus Hygrophorus conicoides Hygrophorus hypothejus Hygrophorus insipidus Hygrophorus langei Hygrophorus niveus Hygrophorus obrusseus Hygrophorus quietus Hygrophorus virgineus Hypholoma fasciculare Hypholoma sublateritium Hypsizygus marmoreus Inocybe agardhii Inocybe dulcamara Inocybe fastigiata n.s. n.s. Big laughing gym Chestnut bolete n.s. n.s. White saddle/Elin saddle/Common helvel n.s. Black elin saddle/Slate grey saddle Berded tooth/Monkey-head mushroom n.s. Hedgehog mushroom/Wood hedgehog Red waxy cap Golden waxy cap False chnterelle n.s. Yellow wax-cap Scarlet waxy cap n.s. Olive-brown waxy cap/Winter herald/Late fall waxy cap n.s. n.s. n.s. n.s. n.s. n.s. Sulphur tuft/Clustered woodlover Bick tops/Brick cap Buno shimeji/Beech mushroom n.s. n.s. Straw-colored iber head Inocybe umbrinella Inonotus dryadeus Ischnoderma resinosum Kuehneromyces mutabilis n.s. Warted oak polypore Resinosum polypore Brown stew fungus/Two-toned pholiota Laccaria amethystina Laccaria laccata Amethyst deceiver Deceiver/Waxy laccaria Laccaria proxima Lactarius blennius Lactarius controversus Lactarius deliciosus Lactarius deterrimus n.s. Slimy milk-cap Willow milky/Poplar milk cap Safron milk cap/Red pine mushroom False safron milk cap/Orange latex milky/Spruce safron lactarius M F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F&M F F F F F F&M F&M Reference(s) Yagi et al. (2000) Pemberton (1994) Devitashvili et al. (2008) Ngai and Ng (2004) Mikiashvili et al. (2006) hakur et al. (2007a); Mikiashvili et al. (2006) Pemberton (1994) Kawagishi et al. (1990); Stepanova, Nikitina, and Boiko (2007) Banerjee et al. (1982) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Kawagishi et al. (1994) Furukawa et al. (1995) Yagi et al.(2000) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Furukawa et al. (1995) Pemberton (1994) Pemberton (1994) Pemberton (1994) Veau et al. (1999) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Pemberton (1994); Coulet, Guillot, and Bétail (1972) Zhao et al. (2009) Pemberton (1994) Kawagishi and Mizuno (1988) Pemberton (1994); Musilek et al. (1990) Pemberton (1994) Ticha, Sychrova, and Kocourek (1988) Pemberton (1994) Pemberton (1994) Pemberton (1994) Guillot et al. (1991) Giollant (1991); Giollant et al. (1993) Table 1. continued on next page 104 Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Table 1. Continued. Source Lactarius luens Lactarius glaucescens Lactarius laeticolor Lactarius lignyotus Common namea n.s. n.s. n.s. Sooty lactarius Lactarius piperatus Lactarius quietus Lactarius rufus Lactarius ruginosus Lactarius salmonicolor Lactarius subvellereus Lactarius subzonarius Lactarius tabidus Lactarius torminosus Peppery milky/Peppery milk mushroom/Hot mother Oakbug milkcap Rufous milkcap n.s. Milk-caps n.s. n.s. Birch milkcap Pink-fringed milky/Wooly milk cap/Bearded milk cap/Poison powderpuf Ugly milk cap n.s. Grey milk cap Weeping milky/Voluminous-latex milky/Orangebrown lactarius Chicken of the woods Shitake mushroom/Japanese forest fungi Lactarius turpis Lactarius vellereus Lactarius vietus Lactarius volemus Location of lectin F F F F F F F F F&M F F F F F F F F Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Lentinus squarrosulus Lentinus torulosus Leotia lubrica Lepiota echinacea Lepiota leucothites (Leucoagaricus leucothitus) Lepiota procera Lepiota rhacodes (Macrolepiota rachodes) Lepista nuda n.s. Twisted panus/Smooth panus/Conch panus Jelly babies Sharp-scaled parasol White dapperling M F F F F Parasol mushroom Shaggy parasol F F Blewit F Linderia bicolumnata Lycoperdon perlatum n.s. Common pufball/Gem-studded pufball/Devil’s snuf-box Clustered domecap/Fried chicken mushroom Honshimeji n.s. Cucumber cap Horsehair fungus n.s. Fairy ring mushroom n.s. Changeable melanoleuca Orange cup Trembling merulius n.s. n.s. Dog stinkhorn n.s. Bleeding mycena Clustered bonnet Grooved bonnet n.s. Sulphur tuft F F Konska et al. (1994) Wang et al. (1999); Tsivileva, Nikitina, and Garibova (2005); Vetchinkina et al. (2008a) Banerjee et al. (1982) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Pemberton (1994); Mikiashvili et al. (2006) Pemberton (1994) Pemberton (1994); Mikiashvili et al. (2006) Pemberton (1994); Mikiashvili et al. (2006) Yagi et al. (2000) Yagi et al. (2000) F F F F F F F F F F F F F F F F F F F F Goldstein et al. (2007) Ng and Lam (2002) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Kruger et al. (2002) Mikiashvili et al. (2006) Pemberton (1994) Ogawa et al. (2001) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Kawagishi et al. (2001) Yagi et al. (2000) Laetiporus sulfureus Lentinus edodes Lyophyllum decastes Lyophyllum shimeiji Lyophyllum sykosporum Macrocystidia cucumis Marasmius androsaceus Marasmius maximus Marasmius oreades Melanoleuca brevipes Melanoleuca melaleuca Melastiza chateri Merulius tremellosus Microporus labelliformis Microporus vernicipes Mutinus caninus Mycena atrocyanea Mycena haematopoda Mycena inclinata Mycena polygramma Mycoleptodonoides aitchisonii Naematoloma fasciculare F F, M & Extracellular Reference(s) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Sychrova, Ticha, and Kocourek (1985) Pemberton (1994) Pemberton (1994); Yagi et al. (2000) Panchak and Antoniuk (2007) Pemberton (1994) Giollant (1991) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Table 1. continued on next page Mushroom lectins 105 Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Table 1. Continued. Source Naematoloma sublateritium Neobulgaria pura Naucoria escharoides Naucoria scolecina Oudemansiella badia Oudemansiella mucida Oudemansiella platyphylla Oudemansiella radicata Panafolus papillionaceus Panellus serotinus Panellus stypticus Panus conchatus Panus tigrinus Paxillus atrotomentosus Paxillus panuoides Paxillus involutus Paxillus xanthophaeus Paecilomyces japonica Perenniporia fraxinea Perenniporia ochroleuca Peziza badia Peziza emileia Peziza praetervisa Peziza sylvestris Phaeolepiota aurea Phallus impudicus Phellinus lundelli Phellinus conchatus Pholiota alnicola Pholiota aurivella Pholiota lammans Pholiota gummosa Pholiota highlandensis Pholiota squarrosa Common namea Brick tops Beech jellydisc Ochre aldercap n.s. n.s. Porcelain mushroom n.s. Rooting shank beech rooter n.s. Late Fall-oyster/Olive oysterling Common stinkhorn n.s. n.s. Fuzzy foot/Velvet-footed pax/Velvet pax Fan pax/Stockless pax Poison pax/Inrolled pax n.s. n.s. n.s. n.s. Bay cup/Pig’s ear n.s. n.s. Brown cup fungus/Fairy tub/Woodland cup Golden false pholiota Stinkhorn n.s. n.s. Golden milk cap Golden pholiota Flaming pholiota/Yellow pholiota n.s. n.s. Scaly pholiota Phylloporus bellus Pisolithus tinctorius Pleurocybella porrigens Pleurotellus porrigens Pleurotus abalonus Pleurotus citrinopileatus Pleurotus cornucopiae n.s. Dead man’s foot Angel wings Angel Wings n.s. Golden oysters Branched oyster fungus Pleurotus eous Pleurotus ostreatus n.s. Black oyster F F Pleurotus serotinus Pleurotus labellatus Pleurotus salmoneostramineus Pleurotus spodoleucus Pleurotus tuber-regium Pluteus cervinus Pluteus chrysophaeus Pluteus depauperatus Pluteus romellii Pluteus salicinus Polyporus adustus n.s. Strawberry oyster n.s. n.s. Sclerotia-forming oyster/King tuber oyster mushroom Deer/Fawn mushroom n.s. n.s. n.s. Willow-shield Smoky polypore F F F F F F F F F F F Location of lectin F F F F F F F F M F F F F F F F F F F F F F F F F F F F F F F F F&M F F F F F F F&M Reference(s) Furukawa et al. (1995) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Matsumoto et al. (2001) Yagi et al. (2000) Banerjee et al. (1982) Yagi et al. (2000) Yagi et al. (2000) Gold and Balding (1975) Yagi et al. (2000) Pemberton (1994) Furukawa et al. (1995) Pemberton (1994) Pemberton (1994) Park et al. (2004) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Wang and Ng (2005) Kawagishi et al. (1996) Entlicher et al. (1985) Pemberton (1994) Pemberton (1994) Pemberton (1994) Kawagishi et al. (1991) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994); Guillot and Konska (1997) Yagi et al. (2000) Yagi et al. (2000) Furukawa et al. (1995) Pemberton (1994) Yagi et al. (2000) Li et al. (2008) Yoshida et al. (1994); Oguri et al. (1996) Mahajan et al. (2002) Conrad and Rudiger (1994); Wang et al. (2000) Gold and Balding (1975) Ho et al. (2004) Yagi et al. (2000) Kogure (1975) Wang, Ng, and Liu (2003) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Wang, Ng, and Liu (2003) Table 1. continued on next page 106 Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur Table 1. Continued. Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Source Polyporus arcularius Polyporus brumalis Polyporus squamosus Polyporus tenuiculus Polyporus varius Psathyrella candolleana Psathyrella piluliformis Psathyrella velutina Pseudotrametes gibbosa Pseudohydnum gelatinosum Psilocybe semilanceata Psilocybe barrerae Pycnoporus coccineus Ramariopsis kunzei Rhizina undulata Rhodophyllus ater Rhodophyllus clypeatus Rozites caperata Russula adusta Russula aeruginea Russula alpina Russula atropurpurea Russula carminea Russula clarolava Russula cyanoxantha Russula farinipes Russula lavida Russula grisea Russula illota Russula laurocerasi Russula nigricans Russula paludosa Russula queletii Russula rosacea Russula sardonia Russula subfoetens Russula vesca Russula violeipes Schizophyllum commune Stereum gausapatum Stropharia aeruginosa Stropharia coronilla Stropharia rugosoannulata Stropharia semiglobata Suillus bovinus Suillus granulatus Termitomyces clypeatus helephora aurantiotincta Trametes hirsutus Trametes versicolor Trichaptum fuscoviolaceum Trichoglossum hirsutum Tricholoma fractum Tricholoma fulvum Tricholoma giganteum Common namea Spring polypore Winter polypore Dryad’s saddle n.s. n.s. Brittle cap/Common psathyrella/Suburban psathyrella Common stump brittlesterm Weeping widow/Velvety psathyrella n.s. Jelly hedgehog Liberty cap n.s. Orange bracket Ivory coral Crust-like cup n.s. Roman shield entoloma Gypsy mushroom Winecork brittlegill Green brittlegill/Tachy green russula n.s. Blackish purple russula/Purple brittlegill n.s. Yellow russula Variegated russula n.s. n.s. Russule grise n.s. Fragrant russula/Almond-scented russula Blackening russula/Blackening brittle gill Tall russule Fruity brittlegill Rosy russula Primrose brittlegill n.s. Bare-toothed russula Velvet brittlegill Split gill Bleeding oak crust/False turkey tail Green Stropharia/Blue-green Stropharia Garland stropharia Wine-cap/Burgundy-cap/Wine cap stropharia Round stropharia/Hemispherical stropharia Jersey cow mushroom Weeping bolete/Granulated bolete/Dotted-stalk suillus n.s. n.s. Hairy turkey tail Turkey tail n.s. Black earth tongue n.s. Birch knight/Yellowbrown knight cap n.s. Location of lectin F F F F F F Reference(s) Yagi et al. (2000) Yagi et al. (2000) Mo, Winter, and Goldstein (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000); Pemberton (1994) F F M F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F F Yagi et al. (2000) Kochibe and Matta (1989) Devitashvili et al. (2008) Pemberton (1994) Pemberton (1994) Hernandez et al. (1993) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Pemberton (1994); Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Han et al. (2005) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) M F F M F F F F F Banerjee et al. (1982) Yagi et al. (2000) Konska (1988) Mikiashvili et al. (2006) Yagi et al. (2000) Pemberton (1994) Mikiashvili et al. (2006) Pemberton (1994) Yagi et al. (2000) Table 1. continued on next page Mushroom lectins 107 Table 1. Continued. Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Source Tricholoma imbricatum Tricholoma mongolicum Tricholoma portentosum Tricholoma saponaceum Tricholoma terreum Tricholoma ustale Tricholoma vaccinum Tricholomopsis decora Tricholomopsis rutilans Tubaria furfuracea Tylopilus valens Tylopilus virens Tyromyces incarnatus Ustulina deusta Volvariella speciosa Volvariella volvacea Xerocomus chrysenteron Common namea Shingled trich n.s. Sooty gray trich/Snow mushroom/Sticky gray trich/ Streaked trich Soapy knight Mouse trich Burnt knight Russet-scaly trich Decorated mop Plums and custard/Red-haired agaric Fringed tubaria/Totally tedious tubaria n.s. n.s. n.s. Carbon cushion Stubble rosegill Straw mushroom/Paddy mushroom Red-cracked bolete Xerocomus spadiceus n.s. Xylaria hypoxylon Carbon antlers/Candlesnuf fungus Xylaria polymorpha Dead man’s ingers Xylobolus princeps n.s. F: Fruiting body; M: Mycelium; n.s.: not speciied. a Source: http//www.allaboutmushrooms.com however, there is no precise correlation between incidence of lectins and systematic groups (Coulet, Mustier, and Guillot, 1970). Although there are many variations in the speciicity and sequences of lectins from mushrooms of the same order or even family, certain species display marked homologies. Lectins from Lactarius deliciosus, L. deterrimus and L. salmonicolor display similar structures and speciicities (Giollant, 1991). A lectin from the fruiting bodies of Melastiza chateri displays sequence similarity to Aleuria aurantia lectin, both belonging to family Pyronemataceae of class Ascomycetes (Ogawa et al., 2001). Lectin with a unique carbohydrate binding speciicity has been isolated from Polyporus squamosus growing on decayed elm stump. his particular lectin has been reported to bind 2000 times more strongly to NeuNAcα2,6Gal3Galβ1,4GlcNAc/Glc than galactose. he lectin did not bind to α2,3 linked sialylated oligosaccharides or glycolipids having α2,3 linked sialic acid nor did it bind to sialic acid itself (Mo, Winter, and Goldstein, 2000). However, lectin isolated from the carpophores of a polypore mushroom Laetiporus sulfureus related to Polyporus squamosus, is completely diferent in its molecular structure, amino acid composition and carbohydrate binding speciicity (Konska et al., 1994). Lectin activity has been reported from fruiting bodies of Mycoleptodonoides aitchisonii of family Climancodontaceae (Kawagishi et al., 2001). Matsumoto et al. (2001) screened 16 mushrooms for lectin activity using hybrid glycoprotein and neoproteoglycan probes and puriied a novel GlcNAc speciic lectin from Oudemansiella platyphylla. Location of lectin F M&F F F F F F F F F F F F F F F&M F F F F F Reference(s) Pemberton (1994) Wang et al. (1995, 1998b) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Yagi et al. (2000); Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) She, Ng, and Liu (1998) Sychrova, Ticha, and Kocourek (1985) Liu et al. (2004) Liu et al. (2006) Yagi et al. (2000) Yagi et al. (2000) Lectins are usually composed of 2–4 identical or nonidentical subunits apprehended by noncovalent forces. However, subunits of lectins from Lactarius lignyotus (Sychrova, Ticha, and Kocourek, 1985) and Phallus impudicus are found to be linked by disulphide bridges (Entlicher et al., 1985). Tetrameric lectin, with identical subunits of 16 kDa each, has been puriied from Agaricus blazei (Kawagishi et al., 1988). A monomeric lectin with the molecular weight 23 kDa has been isolated from Auricularia polytricha belonging to subclass Heteromycetidae of class Basidiomycetes (Yagi and Tadera, 1988). Fruiting bodies of Ganoderma capense produce a 114 kDa hexameric lectin with a high ainity to asialo N-linked triantennary glycans (hakur et al., 2007a,b). Certain mushrooms elaborate lectins with otherwise similar properties but diferent electrophoretic mobilities. Four electrophoretically distinguishable isolectins have been isolated from Agaricus bisporus (Sueyoshi, Tsuji, and Osawa, 1985). Two isolectins showing highest sequence homology to Marasmius oreades lectin (Kruger et al., 2002) have been reported from Polyporus squamosus (Tateno, Winter, and Goldstein, 2004). A novel lectin, which could not be inhibited by simple sugars and glycoproteins, with a unique N-terminal sequence unrelated to any of the known lectins but to mitogen-activated protein kinase, has been isolated from the fruiting bodies of Lyophyllum shimeiji (Ng and Lam, 2002). Amino acid sequence of Grifola frondosa lectin has revealed its homology to jacalin-related plant lectins (Nagata et al., 2005). Some of the known mushroom lectins also display tolerance over a wide range of temperature and pH. A lectin has Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. 108 Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur been reported from Ganoderma capense with a remarkable thermostability at 100°C for 1 h and tolerance over a wide pH (4–11) range (Ngai and Ng, 2004). Lectin isolated from edible mushroom Volvariella volvacea was found to be stable up to 80°C and extremes of pH (Lin and Chou, 1984). A 31 kDa lectin stable within pH 6.0–9.1 below 50°C has been puriied from Ascomycete Cordyceps militaris which has been used as nutraceutical and in traditional Chinese medicine for cancer patients in Eastern Asia (Jung et al., 2007; Wong, Wang, and Ng, 2009). Many plant lectins are commercially available and of the known mushroom lectins, Agaricus bisporus lectin is currently marketed by Sigma Aldrich Co., USA and EY Laboratories Inc., USA. Aleuria aurantia lectin is available from Vector Laboratories, Inc., USA. Lectins from Marasmius oreades and Polyporus squamosus are also available commercially from EY Laboratories Inc., USA. Many mushroom lectins have been cloned and homologies were established in their amino acid sequences and molecular structures. Many of them have been expressed in bacteria and eukaryotes, and recombinant lectins studied to determine changes in their carbohydrate binding speciicities, if any. X-ray crystallographic structures of a host of lectins have also been solved at high atomic resolution. he lectin gene from A. aegerita has been cloned and expressed in E. coli BL21 (DE3) strain and rAAL has also been crystallized (Yang et al., 2005a). Aleuria aurantia lectin has been cloned and expressed in E. coli (Fukumori et al., 1989; Olausson et al., 2008) and Pichia pastoris (Amano et al., 2003), and primary structure has been elucidated by Fukumori et al. (1990). Crystallization studies of the lectin have been attempted by Nagata et al. (1991) and Fujihashi et al. (2003). cDNA from Pleurotus cornucopiae mycelial lectin has been expressed in Pichia pastoris (Sumisa et al., 2004). Lectins from fruiting bodies of Flammulina velutipes and P. ostreatus have also been crystallized (Hirano et al., 1987; Chattopadhyay et al., 1999). Kawagishi and coworkers (2000) fed animals with P. ostreatus lectin along with their normal diet and found a remarkable suppression of food intake by the animals. Recombinant lectin from A. aegerita has been expressed in strain BL21 (DE3) of E. coli (Yang et al., 2005b). A β-propeller crystal structure of Psathyrella velutina lectin has been proposed by Cioci et al. (2006) accounting for its multispeciicity to GlcNAc (Kochibe and Matta, 1989), GlcNAcβ1,2Man of deglycosylated N-glycans (Endo et al., 1992), N-acetyl neuraminic acid (Ueda et al., 1999a) and polysaccharides such as heparin and pectin (Ueda et al., 1999b). A novel pore-forming hemolytic lectin from the parasitic mushroom Laetiporus sulfureus speciic for Galβ1,4GlcNAcβ1,3Galβ1,4Glc has been found homologous to bacterial toxins. he lectin has been cloned and characterized (Tateno and Goldstein, 2003). he crystal structure of Aleuria aurantia lectin in complex with fucose reveals that each monomer of the dimeric lectin is composed of a 6-bladed β-propeller fold and a small antiparallel 2-stranded β-sheet. Each subunit harbors ive fucose binding sites (Wimmerova et al., 2003). X-ray crystal structure resolution of Xerocomus chrysenteron lectin reveals a terameric assembly and similarity to actinoporins (Birck et al., 2004). Recently, a lectin has been isolated from Pleurocybella porrigens, belonging to family Tricholomataceae, with the strongest ainity to GalNAc and O-linked glycans. cDNA of the lectin has been cloned and amino acid analysis establishes its relation to ricin B superfamily (Suzuki et al., 2009). Biological action spectrum of mushroom lectins Most lectins agglutinate erythrocytes of all human blood groups without any noticeable speciicity and are referred to as nonspeciic lectins or panagglutinins. Such lectins bind to saccharide receptors present on the surface of all erythrocytes, irrespective of blood group determinants. Speciic lectins, however, bind to saccharide determinants on the eythrocyte surface and are known to preferentially agglutinate eythrocytes of a particular blood type. Sometimes, the susceptibility of erythrocytes to certain lectins increases upon mild treatment with proteolytic enzymes (Sharon and Lis, 1972) or sialidases (Schauer, 1982). Banerjee, Ghosh, and Sengupta (1982) investigated the mycelial extracts of Volvariella volvacea, Termitomyces clypeatus (Heim), Panafolus papillionaceus (Bull. ex. Fr.) Quel, Gymnopilus chrysimyces (Berk), Lentinus squarrosulus (Mont), Coprinus lagopus (Fr.) Fr., and Coprinus atramentarius (Bull. ex. Fr.) Fr. and found all of them to agglutinate sheep erythrocytes. Lectin from T. clypeatus could also agglutinate human type A eythrocytes and C. atramentarius lectin was found to agglutinate type O erythrocytes more readily, while L. squarrosulus lectin agglutinated both B and AB type erythrocytes. Ticha and colleagues (1985) described two lectins from A. aegerita. One was a nonspeciic erythroagglutinin, while the other lectin speciically agglutinated human type A erythrocytes. Fucose-speciic lectin isolated from Laccaria amethystina possesses anti-H properties with agglutination activity more towards type O and subtype A2 erythrocytes (Guillot et al., 1983). In a thorough investigation, Pemberton (1994) surveyed over 403 British species of higher fungi from widespread locations using human red blood cells and rabbit erythrocytes, and found lectin activity in nearly half of the fungi tested. He concluded that lectin activity and speciicity varies with geographical location of the parent species. Blood group O(H) speciic lectins have been reported from Amanita muscaria (Elo, Estalo, and Malmstrom, 1951; Pemberton, 1994), Xylaria polymorpha (Tetry, Sutton, and Moullec, 1954), Phallus impudicus (Entlicher et al., 1985), P. ostreatus (Kogure, 1975), Pleurotus spodoleucus (Kogure, 1975), Pholiota squarrosa, Suillus bovines, Trametes hirsutus (Konska, 1988), and Daedaleopsis confragosa (Pemberton, 1994). Two N-acetyl-D-galactosamine-speciic lectins from Phaeolepiota aurea showed slight preference to type A erythrocytes than O or B (Kawagishi et al., 1996). Lectin from Fomes fomentarius (Pemberton, 1994) and agglutinin from Marasmius oreades (Pemberton, 1994; Winter, Mostafapour, and Goldstein, 2002) have been reported to bind human blood group B-saccharides. In an attempt to identify the Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Mushroom lectins binding site of Marasmius oreades agglutinin (MOA), Rempel et al. (2003) demonstrated the involvement of OH-4 of β-gal residue and OH-2 of α-gal residue in the recognition process. Blood group (A+B) speciic lectin has been isolated from Hygrophorus hypothejus (Elo, Estalo, and Malmstrom, 1951; Guillot and Coulet, 1974; Veau et al., 1999). Lectin from fruiting bodies of toxic mushroom Amanita pantherina showed a remarkable preference to pronase treated type A erythrocytes rather than O or B (Zhuang et al., 1996). Bolesatine, a glycoprotein with lectin-like properties isolated from Boletus satanus has been demonstrated to exhibit nonspeciic hemagglutinating activity to all blood types, the activity being inhibited by D-galactose (Gachet et al., 1996). Type A speciic lectin has been reported from Pseudohydnum gelatinosum (Pemberton, 1994). Furukawa and authors (1995) screened extracts of 833 fungi for hemagglutinins. Almost 50% of the extracts tested produced hemagglutination in human red cells. Some of the species exhibited blood group speciicity. Strong O agglutinins were observed in extracts of Pleurocybella porrigens, Naematoloma sublateritium, and Pholiota squarrosa. Anti-A lectins were found in Hohenbuehelia serotina, Paxillus panuoides, Melanoleuca melaleuca, and Hygrophorus capreolarius, while potent anti-B activity was determined in Clavulinopsis fusiformis. A similar study was conducted by Yagi and colleagues (2000) who investigated fruiting body extracts of 110 species of Japanese higher fungi for lectin activity using typsinized human and rabbit erythrocytes and 94 of them were found to possess lectins, out of which some of them exhibited blood group speciicity. Lectins from Panellus serotinus, Psathyrella piluliformis, Cantharellus cibarius, and Stropharia rugosoannulata were speciic to human A erythrocytes while lectins from Linderia bicolumnata and Phallus impudicus speciically agglutinated type O erythrocytes. Type (O+B) speciicity was detected in extracts of Gyroporus castaneus and Panellus stypticus. Lectins from 21 species were active only against rabbit erythrocytes. Mycelial lectin from Grifola frondosa showed highest agglutination of human type O and rabbit erythrocytes (Stepanova, Nikitina, and Boiko, 2007). A homodimeric lectin with subunit molecular weight of 15.9 kDa from Clitocybe nebularis agglutinates human blood group A erythrocytes with highest ainity, followed by B, O, and bovine erythrocytes. he glycan microarray analysis revealed binding to human blood group A determinant GalNAcα1,3(Fucα1,2) Galβ-containing glycoconjugates and GalNAc (N,N?diacetyl lactose diamine) with high ainity (Pohleven et al., 2009). he biological action spectrum of Basidiomycete and Ascomycete mushrooms is summarized in Tables 2 and 3. Sugar speciicity Gallagher (1984) classiied lectins as endolectins or exolectins depending on whether they recognize complex oligosaccharide sequences or the terminal, nonreducing residues in complex saccharides. he hemagglutination induced by the latter class could be inhibited by simple 109 sugars or their glycosides while the former are essentially inhibited by complex oligosaccharides bearing speciic sequences. Mushroom lectins display a considerable repertoire of carbohydrate speciicities. he sugar speciicity of the known mushroom lectins is listed in Table 4. An endolectin from fruiting bodies of Pholiota aurivella belonging to family Strophariaceae of order Agaricales has been isolated (Kawagishi et al., 1991). Two lectins have been reported from Agaricus edulis with a molecular weight of 60 and 30 kDa, respectively which could not be inhibited by any of the simple sugars tested (Eiler and Ziska, 1980). Lectin with a complex speciicity has been reported from Agaricus campestris to be a nonspeciic agglutinin reacting with erythrocytes and leukocytes from a number of species. he lectin activity could not be inhibited by any of the sugars but was inhibited by a red cell ghost sonic suspension (Sage and Vazquez, 1967; Sage and Connett, 1969). Laccaria amethystina elaborates two momomeric lectins, a 17.5 kDa lectin speciic for lactose while the other 19 kDa lectin is speciic for L-fucose (Guillot et al., 1983). A nonspeciic lectin identifying asialofetuin and desialylated porcine stomach mucin (asialo-PSM) has been reported from fruiting bodies of Xerocomus chrysenteron and Lactarius lignyotus (Sychrova, Ticha, and Kocourek, 1985). Lectin from carpophores of Lactarius deliciosus has been reported to be highly speciic for D-Galβ1,3D-GalNAc (Guillot et al., 1991). Lectins with diferent carbohydrate speciicity have been isolated from A. cylindracea by diferent workers (Yagi et al., 1997; Wang et al., 2002a). Hemagglutinating activity of the former could not be inhibited by lactose, but could be by glycoconjugates containing NeuAcα2,3Galβ1,3GlcNAc/GalNAc sequence with the lactose being a potent inhibitor of the latter. Aleuria aurantia lectin has high ainity for the Fucα1,6GlcNAc present in the core of complex N-glycans (Haselhorst, Weimar, and Peters, 2001). Lectins from Hericium erinaceum (Kawagishi et al., 1994) and Chlorophyllum molybdites (Kobayashi et al., 2004) have been found to speciically recognize N-glycolylneuraminic acid present on glycosides, expressed on human tumors such as colon cancer, retinoblastoma, melanoma, breast cancer, and yolksac tumors. GalNAc speciic lectins have been reported from Ciborinia camelliae (Otta et al., 2002) and Grifola frondosa fruiting bodies (Kawagishi et al., 1990). he lectin isolated from dikaryotic mycelium of G. frondosa did not exhibit any speciicity to free sugars, while linear D-rhamnan was found to completely inhibit the lectin-mediated hemagglutination, with no such efect by free rhamnose, justifying the endo nature of the lectin (Stepanova, Nikitina, and Boiko, 2007), while the one isolated from fruiting bodies was essentially an exolectin (Kawagishi et al., 1990). GlcNAc speciic lectins have been isolated from Pleurotus tuber-regium (Wang and Ng, 2003), Psathyrella velutina (Kochibe and Matta, 1989) and Oudemansiella platyphylla (Matsumoto et al., 2001). Psathyrella velutina lectin exhibits two distinct binding sites with diferent speciicities, one to which polysaccharides heparin/pectin bind and the other recognizing GlcNAc/NeuNAc (Ueda et al., 1999a,b). Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. 110 Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur Table 2. Biological action spectrum of Basidiomycete mushroom lectins. Human Source A B AB Agaricus abruptibulbus + + n.d. Agaricus bisporus + + + Agaricus blazei + + + + + + Agaricus campestrisa + + n.d. Agrocybe aegeritab Agrocybe cylindracea + + n.d. Amanita crocea + + n.d. Amanita muscaria + + n.d. + + n.d. Amanita pantherina* Amanita pseudoporphyria + + n.d. Amanita spissacea + + n.d. + + n.d. Amanita vaginata** Auricularia polytricha + + n.d. + + n.d. Bjerkandera adusta** Boletus edulis + + n.d. Boletus satanus + + + Calvatia caelata + + n.d. Calvatia craniiformis n.d. Cantharellus cibarius + n.d. + + n.d. Chlorophyllum molybditesc Clavicorona pyxidata + + n.d. Clavulinopsis helvola + + n.d. Clitocybe claviceps + + n.d. + + n.d. Clitocybe gibba** + + n.d. Clitocybe nebularisd + + n.d. Collybia acervata** Collybia conluens + + n.d. − − n.d. Collybia dryophila + + n.d. + + n.d. Collybia fusipes** Coltricia cinnamomea + + n.d. − − − Coprinus atramentariuse + + n.d. Coprinus comatus** − − − Coprinus lagopusf Coprinus micaceus + + n.d. Coriolus hirsutus − − n.d. + + n.d. Coriolus versicolor** Cortinarius balteatus − − n.d. Cortinarius salor + + n.d. Crinipellis stipitaria + + n.d. Cryptoporus volvatus − − n.d. Cyathus stercoreus + + n.d. Dacrymyces palmatus − − n.d. Daedalea dickinsii − − n.d. Daedaleopsis tricolor − − n.d. Descolea lavoannulata + + n.d. Elfvingia applanata − − n.d. + + n.d. Entoloma rhodopolium** + + n.d. Entoloma sericatum** + + + Flammulina velutipesg + + n.d. Fomes fomentarius** Galerina fasciculata − − n.d. + + n.d. Ganoderma lucidum* Grifola frondosa (fruiting + + n.d. bodies) O + + + + + + + + + + + + + + + + + − − + + + + + + + + − + + + + + − + − + − + + − + − − − + − + + + + − + + Rabbit + + n.d. + + + − − n.d. + + − + − + n.d. + + + n.d. + + − − n.d. − − + + − + n.d. − n.d. + + − + + + + + + + + + + − − + − + n.d. n.d. Reference(s) Yagi et al. (2000) Sueyoshi, Tsuji, and Osawa (1985) Kawagishi et al. (1988) Sage and Vazquez (1967) Sun et al. (2003) Yagi et al. (1997) Pemberton (1994) Pemberton (1994) Zhuang et al. (1996) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Yagi and Tadera (1988) Pemberton (1994) Zheng et al. (2007) Gachet et al. (1996) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Kobayashi et al. (2004) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Pemberton (1994); Yagi et al. (2000) Pohleven et al. (2009) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Banerjee et al. (1982) Pemberton (1994) Banerjee et al. (1982) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Yatohgo et al. (1988) Pemberton (1994) Yagi et al. (2000) hakur et al. (2007a) Kawagishi et al. (1990); Nagata et al. (2005) Table 2. continued on next page Mushroom lectins 111 Table 2. Continued. Human Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Source Grifola frondosa (mycelia) A n.d. B n.d. AB n.d. O + Rabbit + Gymnopilus chrysimycesh Gymnopilus liquiritiae Hericium erinaceumi Hydonum repandum Hygrocybe coccinea Hygrocybe lavescens Hygrophoropsis aurantiaca** Hygrophorus chlorophanus** Hygrophorus conicoides** Hygrophorus hypothejus Hygrophorus niveus** Hypsizygus marmoreus Inocybe agardhii** Ischnoderma resinosum Laccaria amethystina (LAL) Laccaria amethystina (LAF) Lactarius deliciosus Lactarius deterrimus Lactarius laeticolor Lactarius lignyotus − + + + + + + + + + + + + + − + + + + + − + + + + + + + + + + + + + − − + + + + − n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. − − n.d. + n.d. + − + + + + + + + + − + + + + + + + + + + n.d. + n.d. + + + − − − n.d. − + − n.d. − − n.d. n.d. + n.d. Lactarius quietus Lactarius rufus Lactarius subvellereus Lactarius subzonarius Lactarius turpis** Laetiporus sulfureus Lentinus squarrosulusj Lentinus torulosus** Lepiota echinacea** Lepiota leucothites Lycoperdon perlatum Lyophyllum sykosporum Macrocystidia cucumis** Marasmius maximus Marasmius oreadesk + + + + + + − + + − − + + − − + + + + + + + + + − − + + − + n.d. n.d. n.d. n.d. n.d. + + n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. + + + + + + − + + − − + + − − + + + + − n.d. n.d. − − + + + − + + Merulius tremellosus** Microporus labelliformis Microporus vernicipes Mutinus caninus Mycena atrocyanea Mycena haematopoda Mycena inclinata** Mycoleptodonoides aitchisonii** Naematoloma fasciculare Naucoria escharoides** Naucoria solecina** Neobulgaria pura Oudemansiella mucida Oudemansiella radicata Paecilomyces japonical + + + + − + + + + + + + − + + + n.d. n.d. n.d. n.d. n.d. n.d. n.d. + + + + + − + + + + + + + + + − n.d. + + + + − + + + + + + − + + n.d. n.d. n.d. n.d. n.d. n.d. n.d. + + + + − + + + − − + + + + Reference(s) Stepanova, Nikitina, and Boiko (2007) Banerjee et al. (1982) Yagi et al. (2000) Kawagishi et al. (1994) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Pemberton (1994) Veau et al. (1999) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Kawagishi and Mizuno (1988) Guillot et al. (1983) Guillot et al. (1983) Guillot et al. (1991) Giollant et al. (1993) Yagi et al. (2000) Sychrova, Ticha, and Kocourek (1985) Pemberton (1994); Yagi et al. (2000) Panchak and Antoniuk (2007) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Konska et al. (1994) Banerjee et al. (1982) Pemberton (1994) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Winter, Mostafapour, and Goldstein (2002) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Kawagishi et al. (2001) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Park et al. (2004) Table 2. continued on next page 112 Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur Table 2. Continued. Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Human Source Panafolus papillionaceusm Panus tigrinus Paxillus involutus Perenniporia fraxinea Perenniporia ochroleuca Phellinus conchatus** Phellinus lundellii** Pholiota aurivella Pholiota squarrosa A − + + + + + + + + B − + + + + + + + + AB − n.d. n.d. n.d. n.d. n.d. n.d. + n.d. O − + + + + + + + + Rabbit n.d. + − + + − −− n.d. + Phylloporus bellus Pisolithus tinctorius Pleurotus salmoneostramineus Pleurotus abalonus Pleurotus eousn Pleurotus ostreatus Pluteus depauperatus*** Pluteus xanthophaeus** Polyporus arcularius Polyporus brumalis Polyporus squamosus Polyporus tenuiculus Polyporus varius Psathyrella candolleana Pseudohydnum gelatinosum Pycnoporus coccineus Ramariopsis kunzei Rhodophyllus ater Rhodophyllus clypeatus Rozites caperata Russula lavida Russula laurocerasi Russula alpina** Russula nigricans Russula rosacea Russula sardonia*** Russula violeipes Stereum gausapatum Suillus bovinus Suillus granulatus Termitomyces clypeatuso helephora aurantiotincta Trichaptum fuscoviolaceum Tricholoma giganteum Tricholoma imbricatum** Tricholoma saponaceum Tricholoma terreum** Tricholoma ustale Tricholoma vaccinum** Tricholomopsis rutilans Tylopilus valens Tylopilus virens Tyromyces incarnatus Ustulina deusta** Volvariella speciosa + + + + − + + + + + + − + + + + + + + + + + + + + + − − − + + + − − + − + + + + − + + + + + + + + − + + + + + + − + + + + + + + + + + + + + + + − − + − + − − + − + + + + − + + + + n.d. n.d. n.d. n.d. − n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. − n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. + + + + − + + + + + + − + + + + + + + + + + + + + + + − − + − + − − + − + + + + − + + + + + + + + + + + + + + + + + + − + + + + + + + − + + − − + + + n.d. + + + − + − + − + + + + − − Reference(s) Banerjee et al. (1982) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Kawagishi et al. (1991) Pemberton (1994); Furukawa et al. (1995) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Mahajan et al. (2002) Kawagishi et al. (2000) Pemberton (1994) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Mo, Winter, and Goldstein (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Banerjee et al. (1982) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Pemberton (1994) Table 2. continued on next page Mushroom lectins 113 Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Table 2. Continued. Human Source A B AB O Rabbit Reference(s) + + + + n.d. Lin and Chou (1984) Volvariella volvaceap Xylobolus princeps + + n.d. + + Yagi et al. (2000) n.d.: not determined. a Hemagglutination also with mouse, rat, cow, sheep, necturius, chicken, bullfrog, turtle, black snake, pigeon erythrocytes b Hemagglutination also with mouse, frog, sheep, cow, chicken, turtle, ish, loach, white eel, yellow eel, duck erythrocytes c Hemagglutination also with pig erythrocytes d Hemagglutination also with bovine erythrocytes e Hemagglutination also with rat and sheep erythrocytes f Hemagglutination also with guinea pig and sheep erythrocytes g Hemagglutination also with equine and porcine erythrocytes h Hemagglutination also with rat, mouse, guinea pig and sheep erythrocytes i Hemagglutination also with pig erythrocytes j Hemagglutination also with rat, mouse, guinea pig and sheep erythrocytes k Hemagglutination also with pig, horse erythrocytes l Hemagglutination also with rat and mouse erythrocytes m Hemagglutination also with rat, mouse, guinea pig and sheep erythrocytes n Hemagglutination also with horse erythrocytes o Hemagglutination also with rat, mouse, guinea pig, goat and sheep erythrocytes p Hemagglutination also with rat, mouse, guinea pig, duck, cat, dog and frog erythrocytes * Hemagglutination only with pronase treated erythrocytes ** Hemagglutination only with bromelin treated erythrocytes *** Hemagglutination with neuraminidase treated erythrocytes Table 3. Biological action spectrum of Ascomycete mushroom lectins. Human Source A B AB Aleuria aurantia + + n.d. Ascoclavulina sakaii + + n.d. Ascocoryne cylichnium + + n.d. − − − Cordyceps militarisq Leotia lubrica + + n.d. Peziza praetervisa + + n.d. Xylaria polymorpha + + n.d. Xylaria polymorpha − − n.d. n.d.: not determined. q Hemagglutination also with rat and mouse erythrocytes Carbohydrate binding speciicity of P. ostreatus was analyzed by surface plasmon resonance. he lectin had high ainity to galactosyl residues and the speciicity has been demonstrated to increase by substitution of galactosyl residue at C-2 position with fucosyl or acetylamino groups (Kobayashi et al., 2005). Lectins from Agaricus bisporus (Carrizo et al., 2005) and Xerocomus chrysenteron (Damian et al., 2005) bind homsen Friedenreich (TF) antigen with strong ainity. X-ray crystallographic structure of A. bisporus lectin reveals the presence of two binding sites in a single domain, which discriminate monosaccharides difering in the coniguration of a single epimeric hydroxyl group. One site binds to Galβ1,3GalNAc and GalNAc while the other is speciic for GlcNAc (Carrizo et al., 2005). Lectin from Boletopsis leucomelas binds with high ainity to biantennary structures with terminal GlcNAc residues. he lectin has a unique speciicity to GlcNAcβ1,2Manα1,3(GlcNAcβ1,2Manα1,6)Man β1,4GlcNAcβ1,4GlcNAc, agalacto structure of biatennary chain of N-linked glycans, as demonstrated using frontal ainity chromatography (Koyama et al., 2006). O + + + − + + + − Rabbit + + + − + + + + Reference(s) Kochibe and Furukawa (1980) Yagi et al. (2000) Yagi et al. (2000) Jung et al. (2007) Yagi et al. (2000) Yagi et al. (2000) Pemberton (1994) Yagi et al. (2000) Certain mushroom lectins are known to display rare carbohydrate speciicities. Inulin speciic lectin has been characterized from fruiting bodies of Xerocomus spadiceus (Liu, Wang, and Ng, 2004). D-Melibiose speciic lectin has been demonstrated from mycelia of Lentinus edodes growing in submerged culture on a lignin-containing medium (Vetchinkina et al., 2008b). Polyporus adustus lectin demonstrates unique speciicity to turanose (Wang, Ng, and Liu, 2003). Peziza sylvestris fruiting bodies elaborate an arabinose speciic lectin (Wang and Ng, 2005). A nonspeciic hexameric lectin with a subunit molecular weight of 17 kDa isolated from fruiting bodies of Lactarius rufus was found to be inhibited by α-phenyl-N-acetylD-glucosaminopyranoside and 4-nitrophenyl-β-Dglucosamine (Panchak and Antoniuk, 2007). Marasmius oreades (Winter, Mostafapour, and Goldstein, 2002) and Lyophyllum decastes (Goldstein et al., 2007), belonging to family Tricholomataceae of Basidiomycetes, are known to produce α-galactosyl binding lectins. M. oreades recognizes the sequence Galα1,3Galβ1,4Glc/ GlcNAc in glycoconjugates, while L. decastes preferably 114 Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Table 4. Speciicity of mushroom lectins. Source Inhibitory sugar/glycoprotein Agaricus bisporus Galβ1,3GalNAc (TF antigen) and Sialyl Galβ1,3GalNAc Agaricus blazei BSM, asialo-BSM, Fetuin, Asialofetuin, GalNAc Agrocybe aegerita Lactose, BSM, Glycophorin A, κ-Casein, Hog gastric mucin β-Galactosides Agrocybe cylinderacea Trisaccharides containing NeuAc-α2,3Galβ-(sialic acid) Agrocybe cylinderacea Sialic acid, Inulin, Lactose, β-Galactosyl residues, Sialoglycoconjugates containing trisaccharide NeuAc-α2,3-gal Aleuria aurantia L-Fucose and Fucosyl oligosaccharides Amanita muscaria Amanita pantherina Amanita phalloides Armillaria luteo-virens Auricularia muscaria Auricularia polytricha Boletus edulis Boletus satanus Boletus subtomentosus Chlorophyllum molybdites Ciborinia camelliae Clitocybe nebularis Coprinus atramentarius Cordyceps cinereus Cordyceps militaris Flammulina velutipes Fomes fomentarius Ganoderma capense Ganoderma lucidum Grifola frondosa Hericium erinaceum Hygrophorus hypothejus Inocybe fastigiata Ischnoderma resinosum Kuehneromyces mutabilis Laccaria amethystina LAF Laccaria amethystina LAL Laccaria laccata Lactarius deliciosus Lactarius deterrimus Lactarius lignyotus Lactarius rufus Lactarius salmonicolor Lactarius vellereus Laetiporus sulfureus O-type glycans Saccharides containing GlcNAcβ1,4Manβ1,4-Pnp, Galβ1,4GlcNAcβ1,4GlcNAc, Galβ1,4(GlcNAc)2β1,4GlcNAc, BSM, asialo-BSM Ovomucin, Human glycophorin A Inulin O-linked glycans Rainose, Galactose, Ovomucoid and β-anomers of galactoside (Lactose, p-Nitrophenyl-β-D-galactoside) D-Xylose and D-Melibiose D-Lactose D-Galactose D-Lactose N-Glycolyl neuraminic acid, GalNAc type residues GalNAc Galβ-, GalNAc D-Lactose β-Galactosides Sialoglycoproteins β-D-Galactosyl residues, Fetuin, Human transferrin, Human glycophorin, Lactoferrin α-D-Galactosyl residues, GalNAc, Rainose D-Galactose, D-Galactosamine O- and N-linked glycans Terminal GalNAc residues Porcine stomach mucin Linear D-rhamnan Sialic acid especially N-glycolyl neuraminic acid Lactose, D-galactose, D-GalNAc, D-Gal-β1,4-D-GlucNAc, o-Nitrophenyl-α-D-GalNAc, p-Nitrophenyl-β-D-GalNAc, asialoBSM GalNAc Methyl-β-galactoside, Fucose, L-Arabinose Asialo-PSM, Asialofetuin, Fetuin, α1 acid glycoprotein, Ovomucoid L-Fucose D-Lactose, GalNAc L-Fucose D-Gal-β1,3-D-GalNAc (TF antigen) D-Gal- β1,3-D-GalNAc (TF antigen) Asialofetuin, asialo-PSM and other desialyzed glycoproteins α-Phenyl-N-acetyl-D-glucosaminopyranoside, 4-nitrophenyl-βD-Glucosamine, asialo-BSM, Human and bovine thyroglobulin, Group speciic substances from human erythrocytes D-Gal- β1,3-D-GalNAc (TF antigen) GalNAc LacNAc and related sugars as L-Rhamnose, Salicine, asialo-BSM, BSM, Asialofetuin Reference(s) Yu et al. (1993); Batterbury et al. (2002) Kawagishi et al. (1988) Sun et al. (2003) Yang et al. (2005a) Yagi et al. (1997) Wang et al. (2002a); Yagi et al. (2001) Kochibe and Furukawa (1980); Olausson et al. (2008) Lutsik-Kordovsky, Stasyk, and Stoika (2001) Zhuang et al. (1996) Lutsik-Kordovsky, Stasyk, and Stoika (2001) Feng et al. (2006) Lutsik-Kordovsky, Stasyk, and Stoika (2001) Yagi and Tadera (1988) Zheng et al. (2007) Colceag, Mogos, and Hulea (1984) Licastro et al. (1993) Colceag, Mogos, and Hulea (1984) Kobayashi et al. (2004) Otta et al. (2002) Horejsi and Kocourek (1978); Pohleven et al. (2009) Colceag, Mogos, and Hulea (1984) Cooper et al. (1997) Jung et al. (2007) Yatohgo et al. (1988); Ng, Ngai, and Xia (2006) Horejsi and Kocourek (1978) Ngai and Ng (2004) hakur et al. (2007a, b) Kawagishi et al. (1990) Nagata et al. (2005) Stepanova, Nikitina, and Boiko (2007) Kawagishi et al. (1994) Veau et al. (1999); Guillot and Coulet (1974) Coulet, Guillot, Bétail (1972) Kawagishi and Mizuno (1988) Musilek et al. (1990) Guillot et al. (1983) Guillot et al. (1983) Ticha, Sychrova, and Kocourek (1988) Guillot et al. (1991) Giollant et al. (1993) Sychrova, Ticha, and Kocourek (1985) Panchak and Antoniuk (2007) Giollant (1991) Coulet, Guillot, Bétail (1972) Konska et al. (1994) Table 4. continued on next page Mushroom lectins 115 Table 4. Continued. Source Lentinus edodes Melastiza chateri Mycoleptodonoides aitchisonii Oudemansiella platyphylla Inhibitory sugar/glycoprotein GlcNAc, GalNAc, Mannose D-Melibiose Galactosyl and glucosyl residues Galα1,4Gal; α-Galactosyl residues at the nonreducing terminal Galα1,3Galβ1,4GlcNAc trisaccharide sequence; Blood group B trisaccharide (Galα1,3Gal2,1αFuc) L-Fucose and Fucosyl residues Asialo-BSM, BSM Terminal GlcNAc Paecilomyces japonica Panus conchatus Paxillus involutus Peziza sylvestris Pholiota aurivella Pholiota squarrosa Sialoglycoproteins D-Galactose Asialo-PSM, Asialofetuin, Fetuin, α1 acid glycoprotein L-Arabinose Fetuin and Asialofetuin L-Fucose Pleurotus citrinopileatus Inulin, o/p-Nitrophenyl-β-D-glucuronide, o-Nitrophenyl-β-Dgalactopyranoside, Maltose GalNAc and O-linked glycans Methyl-α-D-galactoside, Galactosamine, Mannosamine, Asialofetuin D-Melibiose, D-Galactose, Rainose, NeuNAc, Inulin, Lactose Galactosyl and N-Acetyl galactosaminyl groups, BSM, asialoBSM 2?Fucosyllactose GalNAc GlcNAc D-Melibiose, D-Fructose, D-Arabinose, D-Glucose, D-Rainose, Turanose, p-Nitro-α-D-glucopyranoside NeuNAcα2,6βgalactosyl residues Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Lyophyllum decastes Marasmius oreades Pleurocybella porrigens Pleurotus eous Pleurotus ostreatus Pleurotus serotinus Pleurotus tuber-regium Polyporus adustus Polyporus squamosus Psathyrella velutina Psilocybe barrerae Russula nigricans Schizoplyllum commune Volvariella volvacea Xerocomus chrysenteron Xerocomus spadiceus Xylaria hypoxylon GlcNAc NeuNAc, NeuNAcα2,3GlcNAcβ1,4 branch in trisialyl N-glycans Heparin, Pectin D-Galactose, Glycophorin, BSM, asialo-BSM, Human serum and milk transferrin Asialofetuin, asialo-PSM, Fetuin, Ovomucoid, α1 Acid glycoprotein Galactosyl and N-Acetyl galactosaminyl groups hyroglobulin Asialofetuin, asialo-PSM and other desialyzed glycoproteins GalNAc and Gal TF antigen Inulin Xylose, Inulin binds to Galα1,4Gal sequence, which is relatively rare in humans. his disaccharide is also the receptor for various pathogenic bacteria such as E. coli 0157:H7 and Shigella dysenteriae. hus the lectin can be used as a valuable tool for microbiologists and glycobiologists (Goldstein et al., 2007). M. oreades agglutinin contains a ricin B chain-like domain at its N-terminus composed of three subdomains α, β and γ, of which α and γ domains are most probably involved in carbohydrate binding (Tateno and Goldstein, 2004). he crystal structure of MOA with blood group B trisaccharide has been solved at 1.8 Å resolution (Grahn et al., 2009). Reference(s) Wang, Ng, and Ooi (1999) Vetchinkina et al. (2008b) Tsivileva et al. (2000) Goldstein et al. (2007) Loganathan et al. (2003); Winter et al. (2002); Rempel et al. (2003) Ogawa et al. (2001) Kawagishi et al. (2001) Matsumoto et al. (2001); Mikiashvili et al. (2006) Park et al. (2004) Gold and Balding (1975) Ticha, Sychrova, and Kocourek (1988) Wang and Ng (2005) Kawagishi et al. (1991) Coulet, Guillot, Bétail (1972); Ticha, Sychrova, and Kocourek (1988) Li et al. (2008) Suzuki et al. (2009) Mahajan et al. (2002) Wang, Gao, and Ng (2000) Kawagishi et al. (2000) Kogure (1975) Gold and Balding (1975) Wang and Ng (2003) Wang, Ng, and Liu (2003) Mo, Winter, and Goldstein (2000); Zhang et al. (2001); Toma et al. (2001) Kochibe and Matta (1989) Ueda et al. (1999a, 2002) Ueda et al. (1999b) Hernandez et al. (1993) Ticha, Sychrova, and Kocourek (1988) Chumkhunthod et al. (2006) She, Ng, and Liu (1998) Sychrova, Ticha, and Kocourek (1985) Trigueros et al. (2003) Damian et al. (2005) Liu et al. (2004) Liu et al. (2006) Immobilized lectin, from fruiting bodies of polypore mushroom, Polyporus squamosus, has been demonstrated to be speciic for Neu5Acα2,6Galβ1,4Glc/GlcNAc containing oligosaccharides using frontal ainity chromatography (Zhang et al., 2001). Amino acid sequencing and site directed mutagenesis approaches have demonstrated the involvement of β and γ subdomains in sugar binding (Tateno, Winter, and Goldstein, 2004). Devitashvili and colleagues (2008) screened 21 strains of higher basidiomycetes belonging to 16 species of ecologically and taxonomically diferent groups for occurrence of Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. 116 Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur lectins in submerged and solid state fermentation of agroindustrial wastes or by-products and found high hemagglutinating activity in Ganoderma applanatum on lignocellulose, Cerrena unicolor on wheat straw, Funalia trogii on ethanol production residue, Fomes fomentarius and Pseudotrametes gibbosa on wine bagasse. Arabinose and mannose were the potent inhibitors of hemagglutination induced by these lectins. An agglutinin showing speciicity toward β-galactosyl residues has been isolated from the fruiting bodies of Ischnoderma resinosum (Kawagishi and Mizuno, 1988). Chemical modiication and NMR studies revealed the involvement of tyrosine residue in the carbohydrate binding site of the lectin (Kawagishi and Mori, 1991). Galectins constitute a family of genetically related β-galactoside binding lectins mostly identiied from mammalian cells, chicken, eel, frog, nematodes and sponges. hese lectins are also expressed by mushrooms Coprinus cinereus (Cooper et al., 1997), A. cylindracea (Yagi et al., 1997) and A. aegerita (Yang et al., 2005a). A. cylindracea exhibits a unique carbohydrate binding speciicity among the known galectins with resistance to the substitution of 3’O of galactosyl moiety and shows a strong ainity to NeuAcα2,3Lac (Yagi, Hiroyama, and Kodama, 2001). Chemical modiication studies of serine/threonine and histidine amino acids reveal the partial necessity of these residues in the hemagglutinating activity of A. cylindracea lectin (Liu et al., 2008). Mitogenic potential Lectins possess a remarkable property to stimulate the transformation of lymphocytes from small resting cells to large blast-like cells which may undergo mitosis. he most useful outcome of this property has been the examination of biochemical events leading to the conversion of resting cells to actively growing ones (Sharon and Lis, 1972). Activation and proliferation of lymphocytes usually commences by binding of ligands to T-cell receptors, which trigger the signaling cascade, IL-2 gene expression and subsequent proliferation (Nel, 2002). Lectins from Flammulina velutipes (Tsuda, 1979), Armillaria luteo-virens (Feng et al., 2006), Ganoderma capense (Ngai and Ng, 2004), A. cylindracea (Wang et al., 2002a), Xerocomus spadiceus (Liu, Wang, and Ng, 2004), Boletus edulis (Zheng et al., 2007), Cordyceps militaris (Jung et al., 2007), and Pleurotus citrinopileatus (Li et al., 2008) are known to be mitogenic with respect to murine splenocytes. Volvariella volvacea lectin possesses mitogenic activity towards T lymphocytes through T-cell receptor ensuing calcium signaling pathways (Hsu et al., 1997; Ho et al., 2004). Bolesatine from Boletus satanus displays mitogenic activity to human T lymphocytes in vitro (Licastro et al., 1993) and mouse thymocytes in vivo (Ennamany et al., 1994) at low concentration, while high concentration inhibits protein synthesis by interfering with the peptide elongation step (Kretz, Creppy, and Dirheimer, 1991). he mitogenic potential of lectins from mushrooms is detailed in Table 5. Lectins do not always display mitogenic activity to lymphocytes. Certain lectins are demonstrated as antimitogenic. Lectin from Agaricus bisporus suppresses the activation of T and B lymphocytes (Greene, Fleisher, and Waldmann, 1981). Xylaria hypoxylon lectin is known to be antimitogenic to mouse splenocytes (Liu, Wang, and Ng, 2006). However, lectins from Pleurotus labellatus, Hericium erinaceum (Ho et al., 2004), Tricholoma mongolicum (Wang et al., 1995), Laetiporus sulfureus (Konska et al., 1994), and Lactarius deliciosus (Guillot et al., 1991) are nonmitogenic. A lectin, diferent from the earlier report, isolated from Cordyceps militaris was unable to induce mitosis in mouse splenocytes (Wong, Wang, and Ng, 2009). Applications Mushroom lectins are endowed with antiproliferative, antitumor, mitogenic, hypotensive, vasorelaxing, hemolytic, anti-HIV1 reverse transcriptase, and immunepotentiating activities (Li et al., 2008). he ability of lectins to stimulate lymphocytes as well as other cells, have made them important diagnostic and experimental tools to study the Table 5. Mitogenic potential of mushroom lectins. Lectin Source Concentration Cell type Agrocybe cylindracea Mouse splenocytes 2 µM Armillaria luteo-virens Mouse splenocytes 1 µM Boletus edulis Mouse splenocytes 1 µM Cordyceps militaris Mouse splenocytes 26 µM Flammulina velutipes Mouse spleen lymphocytes 100 µg/mL Ganoderma capense Mouse splenocytes 1.5 µM Peziza sylvestris Mouse splenocytes 8 µM Pleurotus citrinopileatus Murine splenocytes 2 µM Polyporus adustus Mouse splenocytes 62.5 µg/mL Schizophyllum commune Mouse splenocytes 4 µM Volvariella volvacea Human peripheral blood 5 µg/mL lymphocytes Xerocomus spadiceus Mouse splenocytes 31.25 µg/mL n.d.: not determined [3H] hymidine incorporated (CPM) 6000 25,000 14,000 n.d. 9.130 ± 580 cpm/well 95,000 ± 5000 23,000 ± 1000 30,000 8,000 23,000 ± 1000 48,000 cpm/well Reference(s) Wang et al. (2002a) Feng et al. (2006) Zheng et al. (2007) Jung et al. (2007) Tsuda (1979); Ng, Ngai, and Xia (2006) Ngai and Ng (2004) Wang and Ng (2005) Li et al. (2008) Wang, Ng, and Liu (2003) Han et al. (2005) Hsu et al. (1997) 23,000 ± 1000 Liu et al. (2004) Mushroom lectins Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. various features of cell growth and diferentiation. Some of the potential applications of mushroom lectins are summarized in Table 6. Lectin from Tricholoma mongolicum possesses antiproliferative, immune potentiating, antitumor, and hypotensive activities (Wang et al., 1996a,b; 1997). Antiproliferative potential Cell surface epitopes undergo changes in glycosylation during transformation of normal cells, which is believed to be correlated to tumor metastasis (Prassanti and Hart, 1988; Hakomori, 1992). Tumor cell surfaces vary in composition of glycoconjugates and their terminal saccharide units (Finne, 1982; Eckhardt and Goldstein, 1983). Lectins may display antiproliferative potential by cross linking the cell surface glycoconjugates or through immunomodulatory efects (Yu et al., 1993; Mody, Joshi, and Chaney, 1995). Volvariella volvacea lectin inhibits cell proliferation of sarcoma S-180 cells (Lin and Chou, 1984) by activating cyclin kinase inhibitors, thereby inhibiting the progression of the cell cycle (Liua, Ho, and Ng, 2001). Lectin from Grifola frondosa is known to be cytotoxic to HeLa cells probably by binding to sugar chains on the cells (Kawagishi et al., 1990). Lectin from Tricholoma mongolicum inhibits mouse mastocytoma PU5-1.8 cells in vitro (Wang et al., 1996a) and sarcoma S 180 cells in Bal b/c mice by modulation of the immune system rather than direct cytotoxicity (Wang et al., 1997). One of the common abnormalities associated with malignant and hyperplastic epithelial cells is increased expression of blood group homsen-Friedenreich antigen (Galactosylβ1,3N-acetylgalactosamine α-). Yu et al. (1993) proposed that lectins recognizing Galβ1,3GalNAc could play a crucial role in determining the rate of proliferation of malignant cells. He reported reversible inhibition of the proliferation of HT29 colon cancer cells, Caco-2 cancer cells, MCF-7 breast cancer cells and Rama-27 rat mammary ibroblasts by homsen-Friedenreich antigen speciic Agaricus bisporus lectin, without any cytotoxic efects. he antiproliferative efect may be a consequence of traicking to the nuclear periphery, where it blocks nuclear localization sequence dependent protein import (Yu et al., 1999). he reversibility of this efect was later attributed to its subsequent slow release from cells after internalization, relecting its tendency to resist biodegradation (Yu, Fernig, and Rhodes, 2000). Agaricus bisporous lectin subdues the growth of human cultured keratinocytes and the human papilloma transformed cell line, thus ofering its implication in situations as psoriasis, where the proliferation of cells is greatly augmented (Parslew et al., 1999). he lectin is also known to inhibit proliferation of Tenon’s capsule ibroblasts in vitro which presents its application in modulating wound healing after glaucoma surgery. he lectin also inhibits collagen lattice contraction without any cytotoxic efect (Batterbury et al., 2002). Amanita phalloides lectin, phallolysin (Lutsik-Kordovsky, Stasyk, and Stoika, 2001) and Flammulina velutipes lectin (Ng et al., 2006) show cytotoxicity to cultured murine leukemia 117 L1210 cells. Phallolysin causes swelling of target cells and their massive lysis after 2 h incubation. Lectin from fruiting bodies of P. ostreatus has been demonstrated as a potent antitumor agent against sarcoma S180 and hepatoma H-22 in mice (Wang, Gao, and Ng, 2000). Pleurotus eous lectin has been reported to exhibit an antiproliferative efect on breast epithelial cell line MCF-7, neuroblastoma cell line SK-N-MC, epidermoid larynx carcinoma cell line HEP-2 and erythroleukemic cell line K562 (Mahajan et al., 2002). Lectin from Xerocomus chrysenteron inhibits proliferation of adherent mammalian cell lines NIH-3T3 and HeLa, with no such efect on nonadherent insect cell line SF 9. It exerts its efect by disrupting cell-matrix interactions, reorganization of actin cytoskeleton, inhibiting cell anchorage and thus preventing proliferation (Marty-Detraves et al., 2004). Damian and co-workers (2005) pointed out that the lectin may have a binding mechanism similar to Agaricus bisporus lectin. Ganoderma capense lectin shows an antiproliferative efect on L1210 and M1 leukemia cells and HepG2 hepatoma cells (Ngai and Ng, 2004). GalNAc speciic lectin from Schizophyllum commune is reported to be cytotoxic against the human epidermoid carcinoma KB cell line (Chumkhunthod et al., 2006). Lectin from Boletopsis leucomelas inhibits the proliferation of human leukemia U 937 cells mainly by inducing apoptosis in the target cells (Koyama et al., 2002). his was by far, the irst report of apoptosis induction by a mushroom lectin. However, the mechanism underlying apoptosis induction by lectins is largely unknown. A. aegerita lectin has also been reported to inhibit proliferation of human tumor cell lines HeLa, SW 480, SGC-7901, MGC 80-3, BGC-823, and HL-60 in vitro and sarcoma S 180 cells in Bal b/c mice by apoptosis induction and DNase activity. he lectin has been cloned and the recombinant lectin although mediating cytotoxic efects by apoptosis induction, lacks DNase activity (Zhao et al., 2003; Yang et al., 2005b). Xylaria hypoxylon lectin possesses antiproliferative activity against M1 and HepG2 tumor cells, the activity being afected by concentration of fetal bovine serum in the medium, as in case of Tricholoma mongolicum lectin (Liu, Wang, and Ng, 2006). Polyporus adustus lectin inhibits the proliferation of tumor cell lines M1, Herto and S180 (Wang, Ng, and Liu, 2003). Sialic acid speciic lectin from Paecilomyces japonica exerts cytotoxic efects on human stomach cancer SNU-1, human pancreas cell AsPc-1 and human breast cancer MDA-MB231 cell lines (Park et al., 2004). Lectin from Armillaria luteovirens is known to inhibit the proliferation of MBL2 cells, HeLa cells and L1210 cells with no such efect on HepG2 cells (Feng et al., 2006). Lectin from wild ascomycete Xylaria hypoxylon exhibits antiproliferative potential against leukemia and hepatoma cell lines with an IC50 of less than 1 µM (Liu, Wang, and Ng, 2006). Cordyceps militaris (Wong, Wang, and Ng, 2008) and Inocybe umbrinella (Zhao et al., 2009a) lectins inhibit the proliferation of HepG2 cells, with the latter being also efective against proliferation of breast cancer MCF7 cells. Lectin from Pleurotus citrinopileatus has been reported to inhibit growth of sarcoma S 180 in ICR mice by 118 Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur Table 6. herapeutic potential of mushroom lectins. Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Source Agaricus bisporus Anti-HIV activity IC50 = 8 µM Boletus edulis Boletus satanas Anti-proliferative activity Inhibits proliferation of HT29 human colon cancer cells, Caco-2 colon cancer cells MCF-7 breast cancer cells, and Rama-27 rat mammary ibroblasts Suppresses DNA synthesis and immunoglobulin production in human T and B lymphocytes Subdues the growth of human cultured keratinocytes and papilloma transformed cell line Inhibits ocular ibroblast proliferation and collagen lattice contraction Strong inhibition of the growth of human tumour cell lines HeLa, SW480, SGC7901, MGC80-3, BGC-823, HL-60, and mouse sarcoma S-180 S-180 tumour cells are also inhibited in vivo Cytotoxic to cultured murine leukemia L1210 cells Antiproliferative to MBL2, HeLa and L1210 cell lines Inhibits proliferation of U937 leukemia cells n.d. n.d. Cordyceps militaris Inhibits proliferation of HepG2 cells IC50 = 10 µM Flammulina velutipes Fip-fve n.d. n.d. Flammulina velutipes lectin Fomitella fraxinea Inhibits proliferation of leukemia L1210 cell line with an IC50 = 13 µM n.d. n.d. Ganoderma capense Inhibits proliferation of L1210, M1, and HepG2 cells Cytotoxicity towards HeLa cell line Inhibits proliferation of HepG2 cells and MCF7 cells with an IC50 = 3.5 and 7.4 µM, respectively Cytotoxic efect on human stomach cancer SNU-1, human pancreas cancer AsPc-1 and human breast cancer MDAMB-231 Inhibits sarcoma 180 in ICR mice 50% growth inhibition of MCF-7, K562, HEP-2 and SK-N-MC cell lines Inhibits sarcoma S180 and hepatoma H-22 in vivo Inhibits M1, Herto, and S180 tumor cell lines Cytotoxic to human epidermoid carcinoma KB cell line Agrocybe aegerita Amanita phalloides Armillaria luteo-virens Boletopsis leucomelas Grifola frondosa Inocybe umbrinella Paecilomyces japonica Pleurotus citrinopileatus Pleurotus eous Pleurotus ostreatus Polyporus adustus Schizophyllum commune Tricholoma mongolicum Inhibits sarcoma180 in vivo and PU5-1.8 cells in vitro Immunomodulatory activity Activates RAW 264.7 macrophages to produce TNFα and nitric oxide Reference(s) Greene, Fleisher, and Waldmann (1981); Yu et al. (1993); Parslew et al. (1999); Wang and Ng (2001); Batterbury et al. (2002); Chang et al. (2007) n.d. n.d. Zhao et al. (2003) n.d. n.d. n.d. n.d. Lutsik-Kordovsky, Stasyk, and Stoika (2001) Feng et al. (2006) n.d. n.d. Koyama et al. (2002) IC50 = 14.3 µM n.d. n.d. Optimal mitogenic doses induce the release of IL-1α and IL-2 from mononuclear cultures n.d. Zheng et al. (2007) Licastro et al. (1993) n.d. Suppresses systemic anaphylaxis reaction and local swelling of mouse foot pads, enhances expression of IL-2 and IFN-γ n.d. Jung et al. (2007); Wong, Wang, and Ng (2009) Ko et al. (1995) Ng et al. (2006) n.d. Enhances MHC-restricted exogenous antigen presentation in antigen presenting cells n.d. Kim et al. (2007) Ngai and Ng (2004) n.d. IC50 = 4.7 µM n.d. n.d. Kawagishi et al. (1990) Zhao et al. (2009) n.d. n.d. Park et al. (2004) IC50 = 0.93 µM n.d. n.d. n.d. Li et al. (2008) Mahajan et al. (2002) n.d. n.d. n.d. n.d. Wang, Gao, and Ng (2000) Wang, Ng, and Liu (2003) IC50 = 1.2 µM n.d. n.d. Enhances TNF production by macrophages in mice Table 6. continued on next page Han et al. (2005); Chumkhunthod et al. (2006) Wang et al. (1996a, 1997) Mushroom lectins 119 Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Table 6. Continued. Anti-HIV activity n.d. Source Volvariella volvacea Fip-vvo Anti-proliferative activity n.d. Volvariella volvacea VVL Xerocomus chrysenteron Arrests cell proliferation of S 180 mouse sarcoma cells Inhibits HeLa and NIH-3T3 cell lines n.d. n.d. Immunomodulatory activity Reduces BSA-induced Arthus reaction in Bal b/c mice and enhances transcriptional expression of IL-2, IL-4, IFN-γ, TNF-α, lymphotoxin and IL-2 receptors Activates h1 cell population by upregulating IFN–γ and IL-2 n.d. Xylaria hypoxylon n.d.: not determined Inhibits M1 and HepG2 cells n.d. n.d. 80% at a dose of 5mg/kg body weight administered daily for 20 days (Li et al., 2008). Antiviral activity A. aegerita lectin inhibits tobacco mosaic virus infection in Nicotiana glutinosa by attaching to TMV particles, thereby blocking the infection site (Sun et al., 2003). Lectins from Agaricus bisporus (Wang and Ng, 2001), Schizophyllum commune (Han et al., 2005), Boletus edulis (Zheng et al., 2007), Pleurotus citrinopileatus (Li et al., 2008), Cordyceps militaris (Wong, Wang, and Ng, 2009) and Inocybe umbrinella (Zhao et al., 2009a) manifest potential inhibition of HIV-1 reverse transcriptase activity with an IC50 of 8 µM, 1.2 µM, 14.3 µM, 0.93 µM, 10 µM, and 4.7 µM, respectively. Immunomodulatory potential Owing to their speciicity to bind to surface receptors, certain lectins are known to activate cascade reactions, culminating in upregulation of the components of the immune system, thereby producing immunomodulatory efects. Bolesatine from Boletus satanus induces the release of IL-1α and IL-2 from mononuclear cell cultures (Licastro et al., 1993). Lectin from Tricholoma mongolicum stimulates nitrite ion production, activates macrophages to produce macrophage activating factor and tumor necrosis factor in C57BL/6 mice (Wang et al., 1996a). Fungal immunomodulatory protein (Fip-fve) from Flammulina velutipes, an edible golden needle mushroom, is known to agglutinate human red blood cells, stimulate human peripheral blood lymphocytes and suppress systematic anaphylaxis reaction and local swelling of mouse foot pads. It also upregulates the transcriptional expression of IL-2 and IFN-γ (Ko et al., 1995) via p38 mitogen-activated protein kinase signaling pathway and triggers IFN-γ releasing h1 cells (Wang et al., 2004). Fipvvo from Volvariella volvacea has been reported to reduce BSA-induced Arthus reaction in Bal b/c mice and enhance the transcriptional expression of IL-2, IL-4, IFN-γ, TNF-α, lymphotoxin, and IL-2 receptor, thus efecting immune modulation via cytokine regulation (Hsu et al., 1997). Lectin VVL from Volvariella volvacea fruiting bodies and mycelium exerts more potent immunomodulatory efect than Fip-vvo, in mice by upregulating the expression of IL-2 and IFN-γ, Reference(s) Hsu et al. (1997) Lin and Chou (1984); She, Ng, and Liu (1998) Marty-Detravis et al. (2004) Liu et al. (2006) thereby upregulating the h-1 cell population (She, Ng, and Liu, 1998). In an attempt to explicate the mechanism underlying its immunomodulatory efect, Sze, Ho, and Liu (2004) performed kinetic analysis of activation markers and demonstrated that the lectin triggers lymphocytes through successive calcium inlux, nuclear localization of nuclear factor of activated T cells, induction of activation markers CD25 and CD69, cytokine production and cell proliferation. Agaricus bisporus lectin shows commendable potential to activate RAW 264.7 macrophages producing TNF-α and nitric oxide (Chang et al., 2007). Lectin from carpophores of Fomitella fraxinea enhances MHC class-I and class-II restricted presentation of exogenous antigen in antigen presenting cells by enhancing the intracellular events of phagocytosed antigens and thus can be used to modulate T cell responses (Kim et al., 2007). Other applications Lectins from Agaricus campestris (Ewart, Kornield, and Kepnis, 1975) and Agaricus bisporus (Ahmad et al., 1984) are known to promote insulin and glucagon production by rat pancreatic Langerhans cells and elevate glucose consumption by adipocytes. Agaricus bisporus lectin immobilized on magnetic beads before PCR assay has been used for the detection of a low number of Bronchothrix in meat samples (Grant et al., 1993). he lectin is also identiied to inhibit contraction and adhesion of human retinal epithelial cells in vitro, without apparent cytotoxicity and can thus, be considered as a potential candidate in prevention and treatment of proliferative vitreoretinopathy and other nonocular wound healing processes (Kent et al., 2003). he lectin recognizes T-antigen which remains hidden in normal cells, but is widely exposed in carcinoma and other neoplastic cells (Springer, 1997) and can be used to diagnose such pathological states. Lectin from Polyporus squamosus speciically recognizes the NeuAcα2,6Galβ1,4Glc/GlcNAc trisaccharide sequence present in N-linked glycans (Mo, Winter, and Goldstein, 2000). NeuAcα2,6GalNAc disaccharide (sialyl Tn antigen) is known to be associated with colon carcinoma (Ogata et al., 1998) and the lectin can be used as a predictive clinical marker in human colorectal carcinoma (Toma et al., 2001). Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. 120 Ram Sarup Singh, Ranjeeta Bhari, and Hemant Preet Kaur So far, some of the plant lectins such as tomato lectin (Naisbett and Woodley, 1995) and Ulex europeus lectin (Lambkin et al., 2003) have been assessed for drug delivery applications. Lectin, from edible orange cup mushroom Aleuria aurantia, has been efectively demonstrated for antigen delivery to M cells in mice. he lectin supported IFN-γ and IgG2a induction, thus opening the perspectives of AAL-functionalized microspheres in oral delivery applications (Roth-Walter et al., 2004, 2005). he structure of AAL closely resembles Salmonella neuraminidase which binds to human M cells (Sansonetti and Phalipon, 1999), the lectin may therefore be used as a means of mucosal targeting in humans. Certain lectins recognize a sequence of saccharides with speciicity towards glycosidic linkages as well as anomeric conigurations and have thus proved to be useful agents for identiication and isolation of carbohydrate residues of glycoconjugates (Goldstein, Winter, and Poretz, 1997). Lectin from Psathyrella velutina is found to exhibit remarkable ainities towards glycoproteins possessing trisialoglycans with α-2,3 linked NeuAc in GlcNAcβ1,4 branch or GlcNAc exposed glycans and thus can be used for separation and detection of sialoglycoconjugates (Ueda et al., 2002). Psathyrella velutina lectin has been shown to preferentially bind to nonreducing GlcNAc residues such as GlcNAcβ1,2Man present in degalactosylated N-glycans (Endo et al., 1992). Such glycosylation changes are associated with inlammatory autoimmune disorders. PVL has been used to detect IgG of rheumatoid arthritis patients (displaying altered glycosylation) by ELISA based assays (Tsuchiya et al., 1993) or ainity biosensor technology (Liljeblad, Lundblad, and Påhlsson, 2000). PVL has also been used to detect altered IgG N-glycans associated with chronic microbial and viral infections as AIDS (Moore et al., 2005). Marasmius oreades agglutinin (MOA) and toxin A produced by Clostridium diicile, responsible for antibiotic-induced diarrhea (Teneberg et al., 1996), recognize the trisaccharide Galα1,3Galβ1,4GlcNAc sequence and thus MOA could possibly compete with toxin A for receptor binding (Winter et al., 2002). his trisaccharide epitope is responsible for hyperacute rejection of xenotransplants from lower mammals to humans, old world monkeys or apes (Loganathan et al., 2003). he authors have proposed lectin ainity chromatography using immobilized MOA for detection, separation and characterization of biomedically important glycoconjugates from human or animal serum. Lectins and hemolysins are accountable for the insecticidal activity of mushroom fruiting bodies and lectin genes from these mushrooms can be expressed in plants to confer insecticidal properties (Wang et al., 2002b). Xerocomus chrysenteron lectin shows insecticidal activity against dipteran Drosophila melanogaster and hemipteran Acyrthosiphon pisum, which can be potentially applied in raising insect resistant transgenic plants (Trigueros et al., 2003). Lectins from Xylaria hypoxylon, Agrocybe cylindracea, Tricholoma mongolicum, Ganoderma cepense, and Boletus edulis have been recently demonstrated to possess antinematode activity against Dictylenchus dispsaci and Heterodera glycines (Zhao et al., 2009b). Future perspectives he ability of lectins to identify subtle variations in carbohydrate structures on the surface of cells and tissues has made them a paradigm to study protein-carbohydrate interactions and is a useful tool in biomedical research, clinical diagnosis and therapy. he sugar speciicity of lectins has led to a better understanding of the function of subcellular mechanisms in diverse ields of biological interest such as pathological markers of diseases, tissue metastasis and for controlling a variety of infections. It has been shown that adhesion of microorganisms to speciic receptors is the initial but essential step in pathological processes. hus adherence of microbes to host cells, leading to colonization, can be disrupted to prevent infections. Blocking the cell receptors using plant lectins or microbial imbriae or adhesins has been achieved in several reports (Driessche et al., 2000). However, binding of lectins to target tissues profoundly afects the metabolism of the host tissues and leads to other physiological conditions such as recruitment of leukocytes to the site of infection (Ofek, Kahane, and Sharon, 1996). Moreover, number and distribution of carbohydrate receptors and their side chains varies according to the physiological state of the host cells. Although signiicant research on lectins during the past decades has advanced the understanding of molecular mechanisms involving recognition and adherence, a number of lacunae still remain to be illed. Better understanding of the atomic structure of lectin-sugar combining sites and molecular mechanisms underlying host-pathogen interactions relevant to in vivo physiology, is expected to provide an efective means of preventing and treating infectious diseases at the molecular level in future. Besides this, lectin histochemistry can be used as a valid tool to better understand etiopathological, morphological and pathological aspects concerning reactivity of lectins to normal or altered glycosylation, as in case of metastatic or neurodegenerative diseases such as Alzheimer’s disease. Sialic acids occupy terminal position on glycoproteins and glycolipids on the surface of vertebrate cells. Sialic acid speciic lectins can be used for detection and preliminary characterization of cell surface sialic acids. Lectin ainity chromatographic approaches can be employed for separation of sialic acids bearing speciic linkages from complex mixtures. Saccharide determinants present on cell surface glycoconjugates serve as important binding sites for speciic lectins, exerting a modulatory efect within the immune system. Such mediating factors with speciic carbohydrate binding eiciencies may be exploited for beneicial manipulations of host’s ability to attack malignant cells (Hajto et al., 1990). Hericium erinaceum lectin recognizes N-glycolylneuraminic acid (Kawagishi et al., 1994), but further speciicity to the type of linkage it recognizes is unknown. To harness the lectins in biological research, binding speciicity towards glycoconjugates needs to be characterized before its successful Critical Reviews in Biotechnology Downloaded from informahealthcare.com by Deakin University on 05/24/10 For personal use only. Mushroom lectins implication to isolate or scrutinize speciic glycoconjugates from mixtures. X-ray crystallographic structures and biochemical properties of the lectins need to be elucidated to fully understand the complex lectin-carbohydrate interactions. Increase in α-2,3 linked sialic acids with increased branching of glycans is observed in hepatocarcinoma (Wang et al., 2009). Owing to its high speciicity, Psathyrella velutina lectin can be used to diagnose changes in the glycosylation pattern (Ueda et al., 2002). Albeit curative roles of many lectins have been ascertained, further pharmacokinetic studies need to be undertaken before their introduction as clinical tools. Newer sources should be explored to isolate novel lectins with potentially exploitable properties. Advancement in genetic engineering techniques now make it possible to obtain cells which express speciic carbohydrates or lectins normally absent in the wild types, which could allow the modiication of social behavior of cells in vitro as well as in vivo. his could prove beneicial to advance diagnosis and treatment of diseases. Although many mushroom lectins have been reported to date, their possible role in vivo remains largely unknown. Further research is needed to establish in vivo beneits of these lectins comparable to their in vitro efects and can then be carried forward for development as dietary supplements or pharmaceuticals. A generalized scheme to explain the diverse roles played by lectins in cell growth and diferentiation is still awaited. Expression of lectins on the surface of cells or diseased tissues ofers a natural means of drug targeting. Coupling a drug via reversible linkage to lectins known to speciically bind to diseased tissues could lead to much higher local tissue levels of the drug and a more eicacious dosage form (Tiwary and Singh, 1999). he selective targeted drug delivery approach by exploiting diferences in receptors expressed on the surface of normal and transformed tissues has been investigated as a means of implementing gene therapy to combat cancer (Batra et al., 1994). Lectins being natural components of the cellular system and biodegradable, and some mushroom lectins such as the plant lectins being stable over a wide range of pH, can be explored for oral drug delivery. Yagi et al. (2000) proposed three families for fungal lectins: irst family incorporates Ganoderma lucidum, Flammulina velutipes, and Volvariella volvacea constituting the immunomodulatory proteins with a molecular weight in the range of 13–16 kDa, second family comprises of 34 kDa Aleuria aurantia lectin whose primary structure has been determined while the third family includes fungal galectins. he Authors realize that the current challenge in this ield remains the elucidation of structure and sequence of already known lectins and the newer ones in order to completely establish families within fungal lectins. Declaration of interest he inancial assistance received from Department of Science and Technology, Govt. of India, New Delhi, under 121 FIST Programme, is duly acknowledged. he authors report no conlicts of interest. References Ahmad N, Bansal R, Ahmad A, Rastogi AK, Kidwai JR. 1984. Puriication of hemagglutinins from Agaricus bisporus by ainity chromatography. Indian J Biochem Biophys 21: 237–240. Amano K, Takase M, Ando A, Nagata Y. 2003. Production of functional lectin in Pichia pastoris directed by cloned cDNA from Aleuria aurantia. Biosci Biotechnol Biochem 67: 2277–2279. Athamna A. 1989a. Annual Meeting of the Israel Society of Microbiology, January 1989 (Abstr.), Haifa, Israel. Athamna A. 1989b. 89th Annual Meeting of the American Society of Microbiology, May 1989 (Abstr. B-104), New Orleans, LA, USA. Banerjee PC, Ghosh AK, Sengupta S. 1982. Hemagglutinating activity in extracts of mycelia from submerged mushroom cultures. Appl Environ Microbiol 44: 1009–1011. 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