A lectin from the mushroom Pholiota aurivella

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.