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    CD4-binding site alterations in CCR5-using HIV-1 envelopes influencing gp120-CD4 interactions and fusogenicity

    Access Status
    Open access via publisher
    Authors
    Sterjovski, J.
    Churchill, M.
    Roche, M.
    Ellett, A.
    Farrugia, W.
    Wesselingh, S.
    Cunningham, A.
    Ramsland, Paul
    Gorry, P.
    Date
    2011
    Type
    Journal Article
    
    Metadata
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    Citation
    Sterjovski, J. and Churchill, M. and Roche, M. and Ellett, A. and Farrugia, W. and Wesselingh, S. and Cunningham, A. et al. 2011. CD4-binding site alterations in CCR5-using HIV-1 envelopes influencing gp120-CD4 interactions and fusogenicity. Virology. 410 (2): pp. 418-428.
    Source Title
    Virology
    DOI
    10.1016/j.virol.2010.12.010
    ISSN
    0042-6822
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/6288
    Collection
    • Curtin Research Publications
    Abstract

    CD4-binding site (CD4bs) alterations in gp120 contribute to different pathophysiological phenotypes of CCR5-using (R5) HIV-1 strains, but the potential structural basis is unknown. Here, we characterized functionally diverse R5 envelope (Env) clones (n = 16) to elucidate potential structural alterations within the gp120 CD4bs that influence Env function. Initially, we showed that the magnitude of gp120-CD4-binding correlates with increased fusogenicity and reduced CD4 dependence. Analysis of three-dimensional gp120 structural models revealed two CD4bs variants, D279 and N362, that were associated with reduced CD4 dependence. Further structural analysis showed that a wider aperture of the predicted CD4bs cavity, as constrained by the inner-most atoms at the gp120 V1V2 stem and the V5 loop, was associated with amino acid alterations within V5 and correlated with increased gp120-CD4 binding and increased fusogenicity. Our results provide evidence that the gp120 V5 loop may alter CD4bs conformation and contribute to increased gp120-CD4 interactions and Env fusogenicity.

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