Lectin from Beauveria bassiana mycelium recognizes Thomsen-Friedenreich antigen and related structures

A lectin was isolated from the mycelium of the stationary growing enthomopathogenic fungus Beauveria bassiana by extraction, chromatography on QAE-Sephadex A-25, salt precipitation, and hydrophobic chromatography on Phenyl-Sepharose 4B. The Beauveria bassiana lectin (BBL) is a 15 kDa glycoprotein rich in hydrophobic amino acids, without detectable amount of methionine. It contains 12.6% of carbohydrates including galactose and mannose. Isoelectric point was found at pH 7.1. The lectin is stable between pH 6 and 11, and at temperature under 50 degrees C. The activity of the lectin was not dependent on with Ca (+ +), Mn (+ +), Mg (+ +) cations and was apparently not blood group ABO specific. The hemagglutination caused by the lectin was inhibited by a lactose (Gal beta 1 --> 4 Glc beta, but not by beta lactose (Gal beta 1 --> 4 Glc beta). In direct ELISA the BBL preferentially reacted with some glycoproteins carrying O-linked sugar structure Gal beta 1 --> 3 GalNAc: strongly with human glycophorin A and weaker with mouse glycophorin, fetuin, IgA, ovine submaxillary mucin. On the other hand BBL did not react in direct ELISA with N-glycoproteins (alpha(1)-acid glycoprotein, haptoglobin, fibronectin), however, N-glycoproteins could act as inhibitors of lectin-glycophorin A interaction. We observed also weak interaction with asialo-Tamm-Horsfall N-glycoprotein having unusual large, branched N-glycans with outer GalNAc beta 1 --> 4Gal sequence. Moreover, the interaction of BBL with highly sialylated preparations of glycoproteins was weaker than with asialo forms. Presented results indicate that BBL exhibits sugar binding specificity towards glycotope corresponding to Thomsen-Friedenreich antigen and its related sequences: Gal beta 1 --> 3 GalNAc > Neu Ac alpha 2-3 Gal beta 1 --> 3 (Neu Ac alpha 2-6) GalNAc > Gal beta 1 --> 4 Glc alpha. (C) 1999 Elsevier Science Inc. All rights reserved.