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Multisite and multivalent binding between cyanovirin-N and branched oligomannosides: Calorimetric and NMR characterization

  1. Author:
    Shenoy, S. R.
    Barrientos, L. G.
    Ratner, D. M.
    O'Keefe, B. R.
    Seeberger, P. H.
    Gronenborn, A. M.
    Boyd, M. R.

  2. Author Address

    NCI, Ctr Canc Res, Mol Targets Discovery Program, Frederick, MD 21702 USA NCI, Ctr Canc Res, Mol Targets Discovery Program, Frederick, MD 21702 USA NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA MIT, Dept Chem, Cambridge, MA 02139 USA Univ S Alabama, Canc Res Inst, Coll Med, Mobile, AL 36688 USA Boyd MR NCI, Ctr Canc Res, Mol Targets Discovery Program, Frederick, MD 21702 USA
    1. Year: 2002
  2. Journal: Chemistry & Biology
    1. 9
    2. 10
    3. Pages: 1109-1118
  4. Type of Article: Article
  1. Abstract:

    Binding of the protein cyanovirin-N to oligomannose-8 and oligomannose-9 of gp120 is crucially involved in its potent virucidal activity against the human immunodeficiency virus (HIV). The interaction between cyanovirin-N and these oligosaccharides has not been thoroughly characterized due to aggregation of the oligosaccharide-protein complexes. Here, cyanovirin-N's interaction with a nonamannoside, a structural analog of oligomannose-9, has been studied by nuclear magnetic resonance and isothermal titration calorimetry. The nonamannoside interacts with cyanovirin-N in a multivalent fashion, resulting in tight complexes with an average 1:1 stoichiometry. Like the nonamannoside, an alpha1-2-linked trimannoside substructure interacts with cyanovirin-N at two distinct protein subsites. The chitobiose and internal core trimannoside substructures of oligomannose-9 are not recognized by cyanovirin-N, and binding of the core hexamannoside occurs at only one of the sites on the protein. This is the first detailed analysis of a biologically relevant interaction between cyanovirin-N and high-mannose oligosaccharides of HIV-1 gp120.

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