9B3E

Crystal structure of a Slam-dependent surface lipoprotein, PmSLP, in Pasteurella multocida

9B3E の概要

• エントリーDOI: 10.2210/pdb9b3e/pdb
• 分子名称: surface lipoprotein, PmSLP-1, SELENIUM ATOM (3 entities in total)
• 機能のキーワード: bacterial surface lipoprotein, complement evasion, membrane protein
• 由来する生物種: Pasteurella multocida 36950
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57305.17

構造登録者

Lai, C.H.R.,Shah, M.,Nguyen, Q.H.,Moraes, T.F. (登録日: 2024-03-19, 公開日: 2025-04-16, 最終更新日: 2025-06-04)

主引用文献

Nguyen, Q.H.,Lai, C.H.R.,Norris, M.J.,Ng, D.,Shah, M.,Lai, C.C.,Isenman, D.E.,Moraes, T.F.
A surface lipoprotein on Pasteurella multocida binds complement factor I to promote immune evasion.
Plos Pathog., 21:e1012686-e1012686, 2025

PubMed Abstract: Pasteurella multocida is the leading cause of wound infections in humans following animals' bites or scratches. This bacterium is also commonly found in the respiratory tract of many mammals and can cause serious diseases resulting in the rapid death of infected animals, especially cattle. To prevent these infections in cattle, a subunit-based vaccine utilizing the surface lipoprotein PmSLP was developed and showed remarkable protection with a single dose administration. Here, we report that PmSLP binds host complement factor I (FI) and facilitates cleavage of complement components C3b and C4b independently of any cofactors (e.g., FH, C4BP), thereby allowing the pathogen to evade host defence. Cryo-EM structure of PmSLP bound to FI reveals that PmSLP stimulates FI enzymatic activity by stabilizing the catalytic domain. This is the first time that a bacterial protein has been shown to directly activate FI independent of complement cofactors and target all arms of the complement cascade.

PubMed: 40327719
DOI: 10.1371/journal.ppat.1012686

実験手法

X-RAY DIFFRACTION (2 Å)