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Title: Proteome-wide mapping of immune features onto Plasmodium protein three-dimensional structures.
Austin Authors: Guy, Andrew J;Irani, Vashti;Beeson, James G;Webb, Benjamin;Sali, Andrej;Richards, Jack S;Ramsland, Paul A 
Affiliation: Life Sciences, Burnet Institute, Melbourne, Australia
Department of Medicine, University of Melbourne, Melbourne, Australia
Department of Microbiology, Monash University, Clayton, Victoria, Australia
University of California, San Francisco, San Francisco, California, USA
Department of Infectious Diseases, Monash University, Melbourne, Australia
Victorian Infectious Diseases Service, Royal Melbourne Hospital, Melbourne, Australia
Department of Immunology, Monash University, Melbourne, Australia
School of Science, RMIT University, Bundoora, Australia
Department of Surgery, Austin Health, The University of Melbourne, Heidelberg, Victoria, Australia
Issue Date: 12-Mar-2018
Date: 2018-03
Publication information: Scientific Reports 2018; 8(1): 4355
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.
DOI: 10.1038/s41598-018-22592-3
ORCID: 0000-0003-3360-4540
Journal: Scientific Reports
PubMed URL: 29531293
Type: Journal Article
Appears in Collections:Journal articles

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