A glucose/mannose-specific lectin (BanLec) was isolated from banana, Musa paradisiaca. BanLec is a dimeric protein that consists of two identical 15 kDa subunits, composed of 141 amino acid residues, and has an isoelectric point of pH 7.3. Based on its crystal structure, this lectin exhibits some uncommon binding properties, as it recognizes 1,3-sugar units at the reducing termini and the internal ?-1,3-linked glucosyl residues. Studies have also shown that BanLec has two primary carbohydrate binding sites per subunit.
BanLec is known to be a potential immunomodulatory molecule and has demonstrated to inhibit HIV-1 by binding directly to gp120 (HIV-1 envelope protein) and being able to block HIV-1 cellular entry. It has a potential anti-viral microbicide that could be used to prevent sexual transmission of HIV-1. BanLec has an activity dependent on metal ions (Ca2+, Mn2+, Mg2+) and exhibits a strong mitogenic activity towards murine T-cells. It is a stable glycoprotein that agglutinates rabbit erythrocytes.
This product comes in a lyophilized form and is stored at -20ë�C. Calcium, manganese, and magnesium ions are required for binding.