Agglutinins (lectins) from some british higher fungi

doi:10.1016/S0953-7562(09)80455-3

Mycological Research

Volume 98, Issue 3, March 1994, Pages 277-290

https://doi.org/10.1016/S0953-7562(09)80455-3 Get rights and content

A total of 403 species of fungi taken from widespread locations were tested for lectins with human and rabbit erythrocytes. Of the 50% which contained agglutinins, few were AB(H) specific serologically: anti-A (Pseudohydnum gelatinosum); anti-B (Fomes fomentarius, Lentinus torlosus and Marasmius oreades) and anti-H (Amanita muscaria and Daedaleopsis confragosa). Clitocybe clavipes and Macrocystidia cucumis showed unusual specificity against enzyme-treated erythrocytes. Mutinus caninus specifically agglutinated rabbit erythrocytes. Heteroagglutinins showed considerable variation in inhibition tests with simple sugars, although Volvariella speciosa was specifically inhibited by N-acetyl-d-galactosamine and Aleuria aurantia and Laccaria amethystea by l-fucose.

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Around 80% of fungal lectins are isolated from mushrooms [13,48]. Over the years, agglutinins have been widely reported from British higher fungi [49], Japanese mushrooms [50,51], Australian mushrooms [52] and South-East Asia mushrooms [53,54]. A wide number of lectins have been reported from edible mushrooms [55–59].
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We strongly advise that A. cylindracea should also be cooked thoroughly before serving like A. aegerita, even it is very necessary to evaluate the food safety of A. cylindracea. Previous studies have shown that about half of known mushrooms are rich in lectins (Pemberton, 1994). Raw dietary and improper processing of fresh edible mushrooms was found to be toxic in rats (Toth et al., 1992).
Edible mushrooms are well-known for their health and nutritional benefits, however, undesirable effects have been reported in animals fed with these types of edible mushrooms (Nieminen et al., 2009). For health and safety reason, it is necessary to evaluate the toxicity of edible mushrooms, especially those that have been artificially cultured in recent decades. The aim of this study was to assess the safety of the edible mushroom Agrocybe aegerita, which is also known as Agrocybe cylindracea in Europe and America. Components from A. aegerita (Yt) were extracted in water and unexpectedly displayed lethal effect and median lethal dose (LD₅₀) at 8.77 g/kg. Strong hepatic toxicity in BALB/c mice was observed when mice were administered with 25 and 250 mg/kg body weight/day of Yt for 6 days. To identify the hepatotoxic components, Yt was further separated into two components by Diaion HP-20 column chromatography to produce the proteins (Yp) and small molecules (Ys) fractions. Biochemical and histopathological analysis showed that Yp could induce liver injury. LC–MS/MS analysis of Yp identified the main causative agent as AAL (A. aegerita lectin), which was shown to have similar hepatotoxicity in the Yt and Yp fractions. In addition, proteinase treatment assays indicated that AAL is resistant to the degradation by digestive enzymes. We have shown that the strong hepatic toxicity is due to a lectin in A. aegerita. This study suggests that correct consumption of A. aegerita can avoid human health risk and help us better understand its nutritional and medicinal value.
A novel glycoprotein from mushroom Hypsizygus marmoreus (Peck) Bigelow with growth inhibitory effect against human leukaemic U937 cells
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Lectins present in many varieties of mushrooms (Feng et al., 2006). They are a glycoprotein with haemagglutinating activity on mammalian erythrocytes (Grahn, Askarieh, & Holmner, 2007; Pemberton, 1994). They may also be inhibitory to the growth of leukaemic cells (Abdullaev & de Mejia, 1997).
This study was to isolate the anti-leukaemic component from edible mushroom Hypsizygus marmoreus (Peck) Bigelow. Crude protein was extracted from the basidioma, and then purified with DEAE-Sepharose CL-6B ion exchange chromatography followed by Sephacryl S-300 gel filtration. A protein which exerted high growth inhibitory effect on human leukaemic U937 cells and sufficient toxicological safety on normal human white blood cells was isolated and named HM-3A. Electrophoresis showed HM-3A approximately 52 kDa in size. N-terminal analysis found the amino acid sequence ATTQWKTSAA and confirmed HM-3A a novel protein. High-performance anion-exchange column chromatography revealed HM-3A a glycoprotein with galactose as the major monosaccharide. Haemagglutination assay proved it non-lectin. We suggest that HM-3A is worth further investigation for antitumour use.
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We have previously reported a novel fungal galectin Agrocybe aegerita lectin (AAL) with apoptosis-induced activity and nuclear migration activity. The importance of nuclear localization for AAL's apoptosis-induced activity has been established by mutant study. However, the mechanism remains unclear.
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Clitocybe nebularis lectin (CNL), a ricin B-like lectin, displays the antiproliferation effect on leukemic T cell lines Mo-T and Jurkat [12]. The investigation on hundreds of fungi containing haemagglutinins by Pemberton [13] has shown that mushroom lectin is a valuable resource for antitumor drug discovery and worth more consideration. However, apart from ABL with the antiproliferation mechanism well defined [14,15], the information about the antitumor mechanism of the mushroom lectins available is still limited.
Agrocybe aegerita lectin (AAL) was identified previously in our group as a novel galectin from medicinal fungi Agrocybe aegerita, and has been shown to effectively induce cancer cell cycle arrest and apoptosis in vitro and tumor regression in vivo. Here, AAL was observed to translocate into the HeLa cell nucleus and induce cell apoptosis when it was predominantly in the nucleus. The N-terminus and C-terminus of AAL were required for nuclear localization. Site mutated proteins were generated based on AAL structure. Dimer interface mutant I25G, carbohydrate recognition domain (CRD) mutant R63H, and loop region mutant L33A could not enter the nucleus and lost the ability to induce apoptosis. CRD mutant H59Q and loop region mutant I144G maintained nuclear localization activity, and H59Q retained residual bioability but I144G had no activity, indicating that nuclear localization is important but not sufficient for AAL to become apoptotically active. Our findings provide a novel antitumor mechanism of fungal galectin.

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View full text

Agglutinins (lectins) from some british higher fungi

Biochimica et Biophysica Acta

Methods in Enzymology

Journal of Biological Chemistry

Journal of Biological Chemistry

Journal of Biological Chemistry

Guidelines for the Blood Transfusion Services in the United Kingdom

Blood group-active surface molecules of the human red blood cell

Vox Sanguinis

Haemagglutinins among higher fungi

Journal of Immunology

Survey of haemagglutinating properties of plant seeds and fungi

Indian Journal of Medical Research

Studies on occurrence and characterization of phytolectins in some species of mushrooms

Revue Roumanie Biochimie

Effects of some mono- and polysaccharides on fungal haemagglutinins

Acta Polonica Pharmacia

fr

Comptes rendus des séances de la Société de Biologie, Paris

fr

Comptes rendus des séances de la Société de Biologie, Paris

fr

Comptes rendus des séances de la Société de Biologie, Paris

fr

Comptes rendus des séances de la Société de Biologie, Paris

fr

Revue de Mycologie

fr

Comptes rendus des séances de la Société de Biologie, Paris

Techniques in Blood Grouping

The lectins from Agaricus edulis, isolation and characterization

Experientia

Phytagglutinins present in Marasmius oreades

Annales medicinae experimentalis et biologiae Fenniae

On phytagglutinins present in mushrooms

Annales medicinae experimentalis et biologiae Fenniae

Studies on lectins. LXIII. Isolation and characterization of a lectin from the stinkhorn mushroom Phallus impudicus L. ex Pers

Weakening of the B-antigen by the presence of A1 as shown by reactions with Fomes fomentarius (anti-B) extract

Vox Sanguinis

Weakening of the B-antigen by the presence of A₁ as shown by reactions with Fomes fomentarius (anti-B) extract