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    Proteome-wide mapping of immune features onto Plasmodium protein three-dimensional structures

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    Author
    Guy, AJ; Irani, V; Beeson, JG; Webb, B; Sali, A; Richards, JS; Ramsland, PA
    Date
    2018-03-12
    Source Title
    Scientific Reports
    Publisher
    NATURE PUBLISHING GROUP
    University of Melbourne Author/s
    Ramsland, Paul; Beeson, James; Richards, Jack; Irani, Vashti
    Affiliation
    Medicine and Radiology
    Surgery (Austin & Northern Health)
    Metadata
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    Document Type
    Journal Article
    Citations
    Guy, A. J., Irani, V., Beeson, J. G., Webb, B., Sali, A., Richards, J. S. & Ramsland, P. A. (2018). Proteome-wide mapping of immune features onto Plasmodium protein three-dimensional structures. SCIENTIFIC REPORTS, 8 (1), https://doi.org/10.1038/s41598-018-22592-3.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/253395
    DOI
    10.1038/s41598-018-22592-3
    Abstract
    Humoral immune responses against the malaria parasite are an important component of a protective immune response. Antibodies are often directed towards conformational epitopes, and the native structure of the antigenic region is usually critical for antibody recognition. We examined the structural features of various Plasmodium antigens that may impact on epitope location, by performing a comprehensive analysis of known and modelled structures from P. falciparum. Examining the location of known polymorphisms over all available structures, we observed a strong propensity for polymorphic residues to be exposed on the surface and to occur in particular secondary structure segments such as hydrogen-bonded turns. We also utilised established prediction algorithms for B-cell epitopes and MHC class II binding peptides, examining predicted epitopes in relation to known polymorphic sites within structured regions. Finally, we used the available structures to examine polymorphic hotspots and Tajima's D values using a spatial averaging approach. We identified a region of PfAMA1 involving both domains II and III under a high degree of balancing selection relative to the rest of the protein. In summary, we developed general methods for examining how sequence-based features relate to one another in three-dimensional space and applied these methods to key P. falciparum antigens.

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