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    A conserved host and pathogen recognition site on immunoglobulins: Structural and functional aspects

    Access Status
    Fulltext not available
    Authors
    Wines, B.
    Trist, H.
    Farrugia, W.
    Ngo, C.
    Trowsdale, J.
    Areschoug, T.
    Lindahl, G.
    Fraser, J.
    Ramsland, Paul
    Date
    2012
    Collection
    • Curtin Research Publications
    Type
    Book Chapter
    Metadata
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    Abstract

    A common site in the constant region (Fc) of immunoglobulins is recognized by host receptors and is a frequent target of proteins expressed by pathogens. This site is located at the junction of two constant domains in the antibody heavy chains and produces a large shallow cavity formed by loops of the CH2 and CH3 domains in IgG and IgA (CH3 and CH4 domains in IgM). Crystal structures have been determined for complexes of IgG-Fc and IgA-Fc with a structurally diverse set of host, pathogen and in vitro selected ligands. While pathogen proteins may directly block interactions with the immunoglobulins thereby evading host immunity, it is likely that the same pathogen molecules also interact with other host factors to carry out their primary biological function. Herein we review the structural and functional aspects of host and pathogen molecular recognition of the common site on the Fc of immunoglobulins. We also propose that some pathogen proteins may promote virulence by affecting the bridging between innate and adaptive immunity.

    Citation
    Wines, B. and Trist, H. and Farrugia, W. and Ngo, C. and Trowsdale, J. and Areschoug, T. and Lindahl, G. et al. 2012. A conserved host and pathogen recognition site on immunoglobulins: Structural and functional aspects, in Lambris, J. and Jajishengallis, G. (ed), Advances in Experimental Medicine and Biology, pp. 87-112. New York: Springer.
    Source Title
    Advances in Experimental Medicine and Biology
    URI
    http://hdl.handle.net/20.500.11937/3090
    DOI
    10.1007/978-1-4614-0106-3_6
    Department
    School of Biomedical Sciences

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