Purification and characterization of a lectin from the mushroom Hypsizigus marmoreus

• A novel lectin, HML, was purified from the edible mushroom Hypsizigus marmoreus by repeated chromatography.
• The molecular weight and partial amino acid sequence of HML were determined.
• The result of the hemagglutination inhibition test suggested that HML belongs to the group with specificity towards N-glycans.

HML (Hypsizigus marmoreus lectin) was isolated from the mushroom Hypsizigus marmoreus using CM cation exchange, bovine submaxillary gland mucin affinity column and TSK-GEL G3000SW gel filtration chromatography. The results of SDS-PAGE, MALDI-TOF MS and gel filtration analysis of HML indicated that the lectin was a dimer with each subunit of 9.5 kDa. The partial amino acid sequences of HML were determined by N-terminal sequencing of peptides obtained by trypsin or Glu-C endopeptidase digest of the lectin. In the hemagglutination inhibition assay, HML did not bind to any mono- or oligo-saccharides tested. Among the glycoproteins examined, asialo-fetuin was the strongest inhibitor.