The role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin griffithsin.

ABSTRACT: Griffithsin (GRFT) is a lectin that has been shown to inhibit HIV infection by binding to high mannose glycan structures on the surface of gp120, and it is among the most potent HIV entry inhibitors reported so far. However, important biochemical details on the antiviral mechanism of GRFT action remain unexplored. In order to understand the role of the three individual carbohydrate-binding sites (CBS) in GRFT, mutations were made at each site (D30A, D70A, and D112A), and the resulting mutants were investigated. NMR studies revealed that each GRFT variant was folded but showed significant peak movement on the carbohydrate-binding face of the protein. The wild-type and each point mutant protein appeared as tight dimers with a K(d) below 4.2 μM. Mutation of any individual CBS on GRFT reduced

SUBMITTER: Xue J 

PROVIDER: S-EPMC3474606 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature