Cellular and Molecular Life Sciences CMLS

, Volume 60, Issue 2, pp 277–287

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

  • I. Botos
  • A. Wlodawer
Multi-author Review

DOI: 10.1007/s000180300023

Cite this article as:
Botos, I. & Wlodawer, A. CMLS, Cell. Mol. Life Sci. (2003) 60: 277. doi:10.1007/s000180300023


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.

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

Copyright information

© Birkhäuser Verlag, 2003

Authors and Affiliations

  • I. Botos
    • 1
  • A. Wlodawer
    • 1
  1. 1.National Cancer Institute, MCL, Bldg. 536, Rm. 5, Frederick, Maryland 21702-1201 (USA), Fax +1 301 846 6128, e-mail: wlodawer@ncifcrf.govUS