4J38

Structure of Borrelia burgdorferi Outer surface protein E in complex with Factor H domains 19-20

4J38 の概要

• エントリーDOI: 10.2210/pdb4j38/pdb
• 関連するPDBエントリー: 2G7I 2M4F 2XQW 3KXV 3KZJ
• 分子名称: Outer surface protein E, Complement factor H, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: beta barrel, immune evasion, complement regulator binding, fh binding, membrane, immune system, erp paralog, lyme disease, bbcrasp-3
• 由来する生物種: Borrelia burgdorferi; 詳細
• 細胞内の位置: Secreted: P08603
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31652.71

構造登録者

Bhattacharjee, A.,Kolodziejczyk, R.,Kajander, T.,Goldman, A.,Jokiranta, T.S. (登録日: 2013-02-05, 公開日: 2013-05-15, 最終更新日: 2024-10-30)

主引用文献

Bhattacharjee, A.,Oeemig, J.S.,Kolodziejczyk, R.,Meri, T.,Kajander, T.,Lehtinen, M.J.,Iwai, H.,Jokiranta, T.S.,Goldman, A.
Structural Basis for Complement Evasion by Lyme Disease Pathogen Borrelia burgdorferi
J.Biol.Chem., 288:18685-18695, 2013

PubMed Abstract: Borrelia burgdorferi spirochetes that cause Lyme borreliosis survive for a long time in human serum because they successfully evade the complement system, an important arm of innate immunity. The outer surface protein E (OspE) of B. burgdorferi is needed for this because it recruits complement regulator factor H (FH) onto the bacterial surface to evade complement-mediated cell lysis. To understand this process at the molecular level, we used a structural approach. First, we solved the solution structure of OspE by NMR, revealing a fold that has not been seen before in proteins involved in complement regulation. Next, we solved the x-ray structure of the complex between OspE and the FH C-terminal domains 19 and 20 (FH19-20) at 2.83 Å resolution. The structure shows that OspE binds FH19-20 in a way similar to, but not identical with, that used by endothelial cells to bind FH via glycosaminoglycans. The observed interaction of OspE with FH19-20 allows the full function of FH in down-regulation of complement activation on the bacteria. This reveals the molecular basis for how B. burgdorferi evades innate immunity and suggests how OspE could be used as a potential vaccine antigen.

PubMed: 23658013
DOI: 10.1074/jbc.M113.459040

実験手法

X-RAY DIFFRACTION (2.83 Å)