ABSTRACT
Eight Fusarium sp. namely, F. acutatum, F. globosum, F. graminearum, F. lactis, F. nivale, F. proliferatum, F.pseudoanthophilum and F. robustum were screened for the presence of lectins by hemagglutination activityusing human ABO, porcine, ovine, goat and rabbit erythrocytes. Mycelial extracts of all the fungal culturesexcept F. graminearum displayed unique lectin activity with only rabbit erythrocytes. Enzymatic treatment ofrabbit erythrocytes with neuraminidase has significantly enhanced the titre of all the lectin-positive extractsof fungal cultures. In contrast, most of the lectins showed a decline in lectin activity with protease treatedrabbit erythrocytes. Saccharide specificity studies have shown that majority of the lectins are inhibitory towardsO-acetyl sialic acids. None of the lectins from Fusarium sp. were inhibited by dextran, meso-inositol, andN-acetyl-D-glucosamine. Most of the fungal cultures displayed highest hemagglutination activity during the10th day of growth in broth cultures. The unique saccharide specificity of Fusarium sp. lectins can be used forelucidating their clinical role in glycobiology research.