Structural highlights
FunctionPublication Abstract from PubMedWe solved the crystal structure of Burkholderia pseudomallei acute phase antigen BPSL2765 in the context of a structural vaccinology study, in the area of melioidosis vaccine development. Based on the structure, we applied a recently developed method for epitope design that combines computational epitope predictions with in vitro 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. Exploiting the Burkholderia pseudomallei acute phase antigen BPSL2765 for structure-based epitope discovery/design in structural vaccinology.,Gourlay LJ, Peri C, Ferrer-Navarro M, Conchillo-Sole O, Gori A, Rinchai D, Thomas RJ, Champion OL, Michell SL, Kewcharoenwong C, Nithichanon A, Lassaux P, Perletti L, Longhi R, Lertmemongkolchai G, Titball RW, Daura X, Colombo G, Bolognesi M Chem Biol. 2013 Sep 19;20(9):1147-56. doi: 10.1016/j.chembiol.2013.07.010. Epub, 2013 Aug 29. PMID:23993463[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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