Abstract
We solved the crystal structure of Burkholderia pseudomallei acute phase antigen BPSL2765 in thecontext of a structural vaccinology study, in the area of melioidosis vaccine development. Based onthe structure, we applied a recently developed method for epitope design that combines computational epitope predictions with invitro mapping experiments and successfully identified a consensus sequence within the antigen that, when engineered as a synthetic peptide, was selectively immunorecognized to the same extent as the recombinant protein in sera from melioidosis-affected subjects. Antibodies raised against the consensus peptide were successfully tested in opsonization bacterial killing experiments and antibody-dependent agglutination tests of B.pseudomallei. Our strategy represents a step in the development of immunodiagnostics, in the production of specific antibodies and in the optimization of antigens for vaccine development, starting from structural and physicochemical principles.
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