Multi-specificities of the N-Acetylglucosamine-Binding Lectin from Psathyrella velutina Mushroom toward Acidic Glycoconjugates

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A lectin from the fruiting body of Psathyrella velutina (PVL) has been reported to be specific for nonreducing terminal N-acetylglucosamine (GlcNAc) residue. PVL was found to exhibit multispecificity toward acidic glycoconjugates, i.e., polysaccharides, sialoglycoproteins, and sulfatide. PVL was purified by single-step affinity chromatography on an N-acetylchitooligosaccharides (GlcNAc_<5-6>)-Sepharose column. The binding specificities of PVL were studied using neoproteoglycans and neoglycoproteins involving heparin or GlcNAc_<5-6>. PVL was shown, by both membrane analysis and solid phase assay, to bind with heparin neoproteoglycans. The binding was inhibited by polygalacturonic acid, dextran sulfate, or fucoidan as well as heparin, but not by GlcNAc, other glycosaminoglycans, colominic acid, or DNA. The pH-dependencies of the binding to heparin and to GlcNAc_<5-6> were different. Biotinylation of PVL destroyed the heparin binding activity while retaining the GlcNAc binding activity. In addition, circular dichroism spectroscopy of PVL indicated that a small conformational change of PVL is induced by binding with GlcNAc but not with heparin, suggesting that the binding sites for acidic polysaccharides and GlcNAc are independently located on PVL. On the other hand. PVL bound to sialoglycoproteins on solid phase assays, and the binding was inhibited with GlcNAc or desialylation treatment, indicating that PVL recognizes N-acetylneuraminic acid residue in glycoproteins at GlcNAc-binding site. The binding of PVL to sulfatide was not inhibited by GlcNAc, N-acetylneuraminic acid, or heparin. These findings indicate that the binding specificities of PVL to glycoconjugates are quite different from those reported for oligosaccharides and PVL is a novel member of muluspecific lectin in higher fungi.
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Multi-specificities of the N-Acetylglucosamine-Binding Lectin from Psathyrella velutina Mushroom toward Acidic Glycoconjugates

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