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. 2003 Feb;60(2):277–287. doi: 10.1007/s000180300023

Cyanovirin-N: a sugar-binding antiviral protein with a new twist

I Botos 1, A Wlodawer 1
PMCID: PMC11138712  PMID: 12678493

Abstract.

Cyanovirin-N (CV-N), an 11-kDa protein from the cyanobacterium Nostoc ellipsosporum, is a highly potent virucidal agent that has generated interest as a lead natural product for the prevention and chemotherapy of human immunodeficiency virus infection. The antiviral activity of CV-N is mediated through specific, high-affinity interactions with the viral surface envelope glycoproteins. A number of structures of wild-type, mutant and sequence-shuffled CV-N have been solved by nuclear magnetic resonance and crystallography, showing that the protein exists as either a quasi-symmetric two-domain monomer or a domain-swapped dimer. Structures of several complexes of CV-N with oligosaccharides help in explaining the unique mode of high-affinity binding of these molecules to both forms of CV-N.

Keywords: Key words. Cyanovirin-N; anti-HIV activity; 3D domain-swapping; gp120; protein folding; X-ray; NMR.

Footnotes

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ID="*"Corresponding author.


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