Purification and characterization of a new lectin from the edible mushroom Boletus edulis with antiproliferative effect on tumor cell lines

CARRIZO, MARÍA E.; BOVI, MICHELE; CAPALDI, STEFANO; PERDUCA, MASSIMILIANO; MONACO, HUGO L.

Pinamar, Buenos Aires, Argentina

Congreso; 10th Congress of the Panamerican Association of Biochemistry and Molecular Biology (PABMB) y XLI Reunión Anual de la Sociedad Argentina de Investigación Bioquímica y Biología Molecular (SAIB); 2005

Sociedad Argentina de Investigación Bioquímica y Biología Molecular (SAIB)

A new lectin was isolated from the fruiting bodies of the edible mushroom Boletus edulis by affinity chromatography on a chitin column. Boletus edulis lectin (BEL) exhibited a molecular mass of approximately 15 kDa in SDS-PAGE under reducing conditions. BEL cDNA was cloned and the deduced primary sequence, corresponding to 142 amino acids and a calculated molecular mass of 15597 Da, showed a high similarity with the members of the fungal saline-soluble lectin family. The binding properties of the lectin were studied by competitive enzyme-lectin assays (CELA). The results show, as it was previously described for the Agaricus bisporus lectin (ABL), that BEL has a binding site with specificity for Thomsen Friedenreich antigen (TF antigen, Galbeta1-3GalNAc related residues. The existence of a second sugar binding site, specific for N-acetyl glucosamine, which we also found in ABL, is under study. The lectin also exhibited a potent dose-dependent antiproliferative activity toward some human tumor cell lines with no apparent cytotoxicity.