Curtin University Homepage
  • Library
  • Help
    • Admin

    espace - Curtin’s institutional repository

    JavaScript is disabled for your browser. Some features of this site may not work without it.
    View Item 
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item

    Structural elements of primary CCR5-using HIV-1 gp120 proteins influencing sensitivity and resistance to the broadly neutralizing monoclonal antibody b12

    Access Status
    Open access via publisher
    Authors
    Sterjovski, J.
    Churchill, M.
    Ellett, A.
    Wesselingh, S.
    Ramsland, Paul
    Gorry, P.
    Date
    2012
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Sterjovski, J. and Churchill, M. and Ellett, A. and Wesselingh, S. and Ramsland, P. and Gorry, P. 2012. Structural elements of primary CCR5-using HIV-1 gp120 proteins influencing sensitivity and resistance to the broadly neutralizing monoclonal antibody b12. Virology. 432 (2): pp. 394-404.
    Source Title
    Virology
    DOI
    10.1016/j.virol.2012.06.024
    ISSN
    0042-6822
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/14643
    Collection
    • Curtin Research Publications
    Abstract

    Structure-guided approaches to HIV-1 vaccine design depend on knowledge of the presentation of neutralizing epitopes on gp120, such as the epitope for the broadly neutralizing mAb b12. Here, we characterized predicted three-dimensional structures of functionally diverse gp120 proteins in their b12-bound conformation, to better understand the gp120 determinants that expose or occlude the b12 epitope. Mapping the gp120-b12 binding interface identified amino acid polymorphisms within the C2, C3, C4 and V5 regions of gp120 associated with augmented b12 binding, and importantly, identified residues in the b12-exclusive binding domain of gp120 that are important for b12 neutralization resistance. Structural studies suggest that these b12 resistance variants promote reduced conformational flexibility in the b12 recognition site, which we show involves structural alterations within the gp120 CD4 binding loop and the V4 loop. Together, our studies provide new mechanistic insights into the gp120 determinants influencing sensitivity and resistance to HIV-1 neutralization by b12. © 2012 Elsevier Inc.

    Related items

    Showing items related by title, author, creator and subject.

    • Structure/function studies of 5a-reductase.
      Baxter, Fiona O. (2001)
      This thesis reports structure-function assessments made using site-directed mutagenesis of the human enzyme 5alpha-reductase (5AR), an enzyme crucial for normal masculine development. These assessments utilised the ...
    • Molecular analysis of genes encoding resistance to Cationic Biocides in staphylococci
      Morgan, Dale (2007)
      Bacterial resistance to non-antibiotic agents is being increasingly studied. Plasmid-mediated resistance to cationic agents, which are important biocides, has been described in antibiotic-resistant Staphylococcus aureus. ...
    • Molecular characterization of Malaysian methicillin-resistant Staphylococcus aureus
      Lim, Tien Tze (2007)
      Seventy-four methicillin-resistant Staphylococcus aureus (MRSA) from two Malaysian hospitals were characterised by both phenotypic and genotypic techniques. These isolates were collected over an 18 year time period in the ...
    Advanced search

    Browse

    Communities & CollectionsIssue DateAuthorTitleSubjectDocument TypeThis CollectionIssue DateAuthorTitleSubjectDocument Type

    My Account

    Admin

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Follow Curtin

    • 
    • 
    • 
    • 
    • 

    CRICOS Provider Code: 00301JABN: 99 143 842 569TEQSA: PRV12158

    Copyright | Disclaimer | Privacy statement | Accessibility

    Curtin would like to pay respect to the Aboriginal and Torres Strait Islander members of our community by acknowledging the traditional owners of the land on which the Perth campus is located, the Whadjuk people of the Nyungar Nation; and on our Kalgoorlie campus, the Wongutha people of the North-Eastern Goldfields.