Purification and partial characterization of carbohydrate-recognition protein C-type lectin from Hemifusus pugilinus.

A mannose binding lectin (C-type lectin) was detected in a molluscan snail Hemifusus pugilinus, this lectin molecule was isolated and purified from the plasma using mannose-fixed sepharose CL-4B column affinity chromatography. The purified protein corresponds to the molecular weight of 118 kDa on an SDS-PAGE gel. The divalent cation-dependent nature of the H. pugilinus lectin (Hp-Lec) evidenced through pH and thermal stability analysis using Circular Dichroism (CD) and Surface Plasmon Resonance (SPR) respectively. Functional investigations of the Hp-Lec reveal a broad spectrum of bacterial agglutination activity against wide range of Gram-positive and Gram-negative bacterial strains. Furthermore, Hp-Lec displayed the haemo agglutination activity against vertebrate red blood cells (RBCs) and its titers were recorded. Excitingly, microbial virulent pathogens such as fungal strains tested against the purified Hp-Lec (25 and 50 μg/ml), which exhibits the effective antifungal activity against tested fungal pathogens such as Aspergillus niger and A. flavus.