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    An altered and more efficient mechanism of CCR5 engagement contributes to macrophage tropism of CCR5-using HIV-1 envelopes

    Access Status
    Open access via publisher
    Authors
    Sterjovski, J.
    Roche, M.
    Churchill, M.
    Ellett, A.
    Farrugia, W.
    Gray, L.
    Cowley, D.
    Poumbourios, P.
    Lee, B.
    Wesselingh, S.
    Cunningham, A.
    Ramsland, Paul
    Gorry, P.
    Date
    2010
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Sterjovski, J. and Roche, M. and Churchill, M. and Ellett, A. and Farrugia, W. and Gray, L. and Cowley, D. et al. 2010. An altered and more efficient mechanism of CCR5 engagement contributes to macrophage tropism of CCR5-using HIV-1 envelopes. Virology. 404 (2): pp. 269-278.
    Source Title
    Virology
    DOI
    10.1016/j.virol.2010.05.006
    ISSN
    0042-6822
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/31354
    Collection
    • Curtin Research Publications
    Abstract

    While CCR5 is the principal coreceptor used by macrophage (M)-tropic HIV-1, not all primary CCR5-using (R5) viruses enter macrophages efficiently. Here, we used functionally-diverse R5 envelope (Env) clones to characterize virus-cell interactions important for efficient CCR5-mediated macrophage entry. The magnitude of macrophage entry by Env-pseudotyped reporter viruses correlated with increased immunoreactivity of CD4-induced gp120 epitopes, increased ability to scavenge low levels of cell-surface CCR5, reduced sensitivity to the CCR5 inhibitor maraviroc, and increased dependence on specific residues in the CCR5 ECL2 region. These results are consistent with an altered and more efficient mechanism of CCR5 engagement. Structural studies revealed potential alterations within the gp120 V3 loop, the gp41 interaction sites at the gp120 C- and N-termini, and within the gp120 CD4 binding site which may directly or indirectly lead to more efficient CCR5-usage. Thus, enhanced gp120-CCR5 interactions may contribute to M-tropism of R5 HIV-1 strains through different structural mechanisms. © 2010 Elsevier Inc.

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