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PDBsum entry 4b5c

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Top Page protein ligands Protein-protein interface(s) links
Lipid transport PDB id
4b5c
Contents
Protein chains
119 a.a.
Ligands
ACT ×3
Waters ×60

References listed in PDB file
Key reference
Title Exploiting the burkholderia pseudomallei acute phase antigen bpsl2765 for structure-Based epitope discovery/design in structural vaccinology.
Authors L.J.Gourlay, C.Peri, M.Ferrer-Navarro, O.Conchillo-Solé, A.Gori, D.Rinchai, R.J.Thomas, O.L.Champion, S.L.Michell, C.Kewcharoenwong, A.Nithichanon, P.Lassaux, L.Perletti, R.Longhi, G.Lertmemongkolchai, R.W.Titball, X.Daura, G.Colombo, M.Bolognesi.
Ref. Chem Biol, 2013, 20, 1147-1156. [DOI no: 10.1016/j.chembiol.2013.07.010]
PubMed id 23993463
Abstract
We 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.
PROCHECK
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