2M6U

NMR Structure of CbpAN from Streptococcus pneumoniae

2M6U の概要

• エントリーDOI: 10.2210/pdb2m6u/pdb
• 関連するPDBエントリー: 4K12
• NMR情報: BMRB: 19155
• 分子名称: Choline binding protein A (1 entity in total)
• 機能のキーワード: three-helix bundle, choline binding protein, choline-binding protein
• 由来する生物種: Streptococcus pneumoniae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9849.24

構造登録者

Liu, A.,Yan, H.,Achila, D.,Martinez-Hackert, E.,Li, Y.,Banerjee, R. (登録日: 2013-04-10, 公開日: 2014-04-16, 最終更新日: 2024-05-15)

主引用文献

Achila, D.,Liu, A.,Banerjee, R.,Li, Y.,Martinez-Hackert, E.,Zhang, J.R.,Yan, H.
Structural determinants of host specificity of complement Factor H recruitment by Streptococcus pneumoniae.
Biochem.J., 465:325-335, 2015

PubMed Abstract: Many human pathogens have strict host specificity, which affects not only their epidemiology but also the development of animal models and vaccines. Complement Factor H (FH) is recruited to pneumococcal cell surface in a human-specific manner via the N-terminal domain of the pneumococcal protein virulence factor choline-binding protein A (CbpAN). FH recruitment enables Streptococcus pneumoniae to evade surveillance by human complement system and contributes to pneumococcal host specificity. The molecular determinants of host specificity of complement evasion are unknown. In the present study, we show that a single human FH (hFH) domain is sufficient for tight binding of CbpAN, present the crystal structure of the complex and identify the critical structural determinants for host-specific FH recruitment. The results offer new approaches to the development of better animal models for pneumococcal infection and redesign of the virulence factor for pneumococcal vaccine development and reveal how FH recruitment can serve as a mechanism for both pneumococcal complement evasion and adherence.

PubMed: 25330773
DOI: 10.1042/BJ20141069

実験手法

SOLUTION NMR