Musa acuminata Lectin (BanLec)
Musa acuminata lectin (BanLec) is isolated from banana pulp and purified by affinity column chromatography on a Mannose-Sepharose 6B-CL gel. This Jacalin-type lectin is a dimeric lectin composed of two identical subunits of 15 kDa.
BanLec shows affinity towards:
- terminal α-D-mannosyl/glycosyl units
- internal α-1,3-mannosyl/glucosyl units
- terminal β-1,3-glucosyl units.
The recognition of both internal 3-O-mannosyl/glucosyl residues and the reducing terminal 3-O-mannosyl/glucosyl unit of oligosaccharides make BanLec unique in its carbohydrate binding properties.
BanLec agglutinates rabbit erythrocytes. Moreover, BanLec has been demonstrated to be a powerful murine Tcell mitogen and also has been shown to stimulate human T-cell profileration.
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.
H. T. Preis