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

被引:51
作者
Botos, I [1 ]
Wlodawer, A [1 ]
机构
[1] Natl Canc Inst, MCL, Frederick, MD 21702 USA
关键词
cyanovirin-N; anti-HIV activity; 3D domain-swapping; gp120; protein folding; X-ray; NMR;
D O I
10.1007/s000180300023
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:277 / 287
页数:11
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