6V3P

The BIgI domain of beta protein from S. agalactiae bound to CEACAM1

6V3P の概要

• エントリーDOI: 10.2210/pdb6v3p/pdb
• 分子名称: Carcinoembryonic antigen-related cell adhesion molecule 1, IgA FC receptor, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: bacterial, adhesin, cell adhesion
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 53244.63

構造登録者

Bonsor, D.A.,McCarthy, A.J. (登録日: 2019-11-26, 公開日: 2020-12-02, 最終更新日: 2023-10-11)

主引用文献

van Sorge, N.M.,Bonsor, D.A.,Deng, L.,Lindahl, E.,Schmitt, V.,Lyndin, M.,Schmidt, A.,Nilsson, O.R.,Brizuela, J.,Boero, E.,Sundberg, E.J.,van Strijp, J.A.G.,Doran, K.S.,Singer, B.B.,Lindahl, G.,McCarthy, A.J.
Bacterial protein domains with a novel Ig-like fold target human CEACAM receptors.
Embo J., 40:e106103-e106103, 2021

PubMed Abstract: Streptococcus agalactiae, also known as group B Streptococcus (GBS), is the major cause of neonatal sepsis in humans. A critical step to infection is adhesion of bacteria to epithelial surfaces. GBS adhesins have been identified to bind extracellular matrix components and cellular receptors. However, several putative adhesins have no host binding partner characterised. We report here that surface-expressed β protein of GBS binds to human CEACAM1 and CEACAM5 receptors. A crystal structure of the complex showed that an IgSF domain in β represents a novel Ig-fold subtype called IgI3, in which unique features allow binding to CEACAM1. Bioinformatic assessment revealed that this newly identified IgI3 fold is not exclusively present in GBS but is predicted to be present in adhesins from other clinically important human pathogens. In agreement with this prediction, we found that CEACAM1 binds to an IgI3 domain found in an adhesin from a different streptococcal species. Overall, our results indicate that the IgI3 fold could provide a broadly applied mechanism for bacteria to target CEACAMs.

PubMed: 33522633
DOI: 10.15252/embj.2020106103

実験手法

X-RAY DIFFRACTION (3.25 Å)