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4B5C

Crystal structure of the peptidoglycan-associated lipoprotein from Burkholderia pseudomallei

4B5C の概要
エントリーDOI10.2210/pdb4b5c/pdb
関連するPDBエントリー4B54
分子名称PUTATIVE OMPA FAMILY LIPOPROTEIN, ACETATE ION (3 entities in total)
機能のキーワードlipid transport, pal-tol complex, acute burkholderia pseuodomallei antigen
由来する生物種BURKHOLDERIA PSEUDOMALLEI
タンパク質・核酸の鎖数3
化学式量合計46163.69
構造登録者
主引用文献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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.3 Å)
構造検証レポート
Validation report summary of 4b5c
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-18に公開中

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