4B5C

Crystal structure of the peptidoglycan-associated lipoprotein from Burkholderia pseudomallei

Summary for 4B5C

• Entry DOI: 10.2210/pdb4b5c/pdb
• Related: 4B54
• Descriptor: PUTATIVE OMPA FAMILY LIPOPROTEIN, ACETATE ION (3 entities in total)
• Functional Keywords: lipid transport, pal-tol complex, acute burkholderia pseuodomallei antigen
• Biological source: BURKHOLDERIA PSEUDOMALLEI
• Total number of polymer chains: 3
• Total formula weight: 46163.69

Authors

Gourlay, L.J.,Peri, C.,Conchillo-Sole, O.,Ferrer-Navarro, M.,Gori, A.,Longhi, R.,Rinchai, D.,Lertmemongkolchai, G.,Lassaux, P.,Daura, X.,Colombo, G.,Bolognesi, M. (deposition date: 2012-08-03, release date: 2013-08-14, Last modification date: 2023-12-20)

Primary citation

Gourlay, L.J.,Peri, C.,Ferrer-Navarro, M.,Conchillo-Sole, O.,Gori, A.,Rinchai, D.,Thomas, R.J.,Champion, O.L.,Michell, S.L.,Kewcharoenwong, C.,Nithichanon, A.,Lassaux, P.,Perletti, L.,Longhi, R.,Lertmemongkolchai, G.,Titball, R.W.,Daura, X.,Colombo, G.,Bolognesi, M.
Exploiting the Burkholderia Pseudomallei Acute Phase Antigen Bpsl2765 for Structure-Based Epitope Discovery/Design in Structural Vaccinology.
Chem.Biool., 20:1147-, 2013

PubMed 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.

PubMed: 23993463
DOI: 10.1016/J.CHEMBIOL.2013.07.010

Experimental method

X-RAY DIFFRACTION (2.3 Å)