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

  1. Author:
    Botos, I.
    Wlodawer, A.

  2. Author Address

    Natl Canc Inst, MCL, Bldg 536, Frederick, MD 21702 USA Natl Canc Inst, MCL, Frederick, MD 21702 USA Wlodawer A Natl Canc Inst, MCL, Bldg 536, Frederick, MD 21702 USA
    1. Year: 2003
  2. Journal: Cellular and Molecular Life Sciences
    1. 60
    2. 2
    3. Pages: 277-287
  4. Type of Article: Review
  1. 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.

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