• Login
    ARAN - Access to Research at NUI Galway
    View Item 
    •   ARAN Home
    • Support Services
    • Externally hosted open access publications with NUI Galway authors (2)
    • View Item
    •   ARAN Home
    • Support Services
    • Externally hosted open access publications with NUI Galway authors (2)
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of ARANCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsTypesThis CollectionBy Issue DateAuthorsTitlesSubjectsTypes

    My Account

    LoginRegister

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Help

    How to submit and FAQs

    Predicting the origins of anti-blood group antibody specificity: a case study of the abo a- and b-antigens

    Thumbnail
    View/Open
    Full Text
    Date
    2014-08-22
    Author
    Makeneni, Spandana
    Ji, Ye
    Watson, David C.
    Young, N. Martin
    Woods, Robert J.
    Metadata
    Show full item record
    Usage
    This item's downloads: 0 (view details)
    Cited 8 times in Scopus (view citations)
    
    Recommended Citation
    Makeneni, Spandana; Ji, Ye; Watson, David C. Young, N. Martin; Woods, Robert J. (2014). Predicting the origins of anti-blood group antibody specificity: a case study of the abo a- and b-antigens. Frontiers in Immunology 5 ,
    Published Version
    http://journal.frontiersin.org/article/10.3389/fimmu.2014.00397/pdf
    Abstract
    The ABO blood group system is the most important blood type system in human transfusion medicine. Here, we explore the specificity of antibody recognition toward ABO blood group antigens using computational modeling and biolayer interferometry. Automated docking and molecular dynamics simulations were used to explore the origin of the specificity of an anti-blood group A antibody variable fragment (Fv AC1001). The analysis predicts a number of Fv-antigen interactions that contribute to affinity, including a hydrogen bond between a His(L49) and the carbonyl moiety of the GaINAc in antigen A. This interaction was consistent with the dependence of affinity on pH, as measured experimentally; at lower pH there is an increase in binding affinity. Binding energy calculations provide unique insight into the origin of interaction energies at a per-residue level in both the scFv and the trisaccharide antigen. The calculations indicate that while the antibody can accommodate both blood group A and B antigens in its combining site, the A antigen is preferred by 4 kcal/mol, consistent with the lack of binding observed for the B antigen.
    URI
    http://hdl.handle.net/10379/12601
    Collections
    • Externally hosted open access publications with NUI Galway authors (2)
    • Copyright @ NUI Galway
    • Library
    • NUI Galway