3ZS6

The Structural characterization of Burkholderia pseudomallei OppA.

3ZS6 の概要

• エントリーDOI: 10.2210/pdb3zs6/pdb
• 分子名称: PERIPLASMIC OLIGOPEPTIDE-BINDING PROTEIN, OLIGOPEPTIDE DVA, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: peptide binding protein, abc transport system
• 由来する生物種: BURKHOLDERIA PSEUDOMALLEI; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57447.60

構造登録者

Lassaux, P.,Gourlay, L.J.,Bolognesi, M. (登録日: 2011-06-23, 公開日: 2012-07-04, 最終更新日: 2024-11-13)

主引用文献

Lassaux, P.,Peri, C.,Ferrer-Navarro, M.,Gourlay, L.J.,Gori, A.,Conchillo-Sole, O.,Rinchai, D.,Lertmemongkolchai, G.,Longhi, R.,Daura, X.,Colombo, G.,Bolognesi, M.
A Structure-Based Strategy for Epitope Discovery in Burkholderia Pseudomallei Oppa Antigen.
Structure, 21:167-, 2013

PubMed Abstract: We present an approach integrating structural and computational biology with immunological tests to identify epitopes in the OppA antigen from the Gram-negative pathogen Burkholderia pseudomallei, the etiological agent of melioidosis. The crystal structure of OppA(Bp), reported here at 2.1 Å resolution, was the basis for a computational analysis that identified three potential epitopes. In parallel, antigen proteolysis and immunocapturing allowed us to identify three additional peptides. All six potential epitopes were synthesized as free peptides and tested for their immunoreactivity against sera from healthy seronegative, healthy seropositive, and recovered melioidosis patients. Three synthetic peptides allowed the different patient groups to be distinguished, underlining the potential of this approach. Extension of the computational analysis, including energy-based decomposition methods, allowed rationalizing results of the predictive analyses and the immunocapture epitope mapping. Our results illustrate a structure-based epitope discovery process, whose application may expand our perspectives in the diagnostic and vaccine design fields.

PubMed: 23159127
DOI: 10.1016/J.STR.2012.10.005

実験手法

X-RAY DIFFRACTION (2.1 Å)