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SubB家族的蛋白质在……中提供多种血清抗性机制。

Proteins of the SubB family provide multiple mechanisms of serum resistance in .

作者信息

Pierre François, Baillez Alexandre, Dewitte Amélie, Rolandelli Agustin, Sebbane Florent

机构信息

Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017 - CIIL - Center for Infection and Immunity of Lille, Lille, France.

出版信息

Emerg Microbes Infect. 2025 Dec;14(1):2493926. doi: 10.1080/22221751.2025.2493926. Epub 2025 May 6.

DOI:10.1080/22221751.2025.2493926
PMID:40237516
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12064104/
Abstract

The serum complement system is a cornerstone element of the innate immune response. Bacterial resistance to this system is a multifaceted process involving various proteins and molecular mechanisms. Here, we report several genes required for the growth of in serum. Among them, we found that encodes an outer-membrane-associated lectin that recruits factor H, C4BP and hemopexin, conferring resistance to the serum complement system. YPO0337 displays high sequence similarity with the SubB subunit of the AB toxin from , as well as other SubB-like proteins, and from restores the ability of Δ mutant to resist to serum complement. Altogether, the data suggest that at least two members of the SubB protein family function as virulence factors, conferring resistance to serum complement through a unique mode of action.

摘要

血清补体系统是先天免疫反应的基石要素。细菌对该系统的抗性是一个涉及多种蛋白质和分子机制的多方面过程。在此，我们报告了在血清中生长所需的几个基因。其中，我们发现 编码一种与外膜相关的凝集素，该凝集素招募因子H、C4BP和血红素结合蛋白，赋予对血清补体系统的抗性。YPO0337与来自 的AB毒素的SubB亚基以及其他SubB样蛋白具有高度序列相似性，并且来自 的 恢复了 Δ突变体抵抗血清补体的能力。总之，数据表明SubB蛋白家族的至少两个成员作为毒力因子发挥作用，通过独特的作用方式赋予对血清补体的抗性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0fd/12064104/f11acd24e195/TEMI_A_2493926_F0004_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0fd/12064104/552cade627be/TEMI_A_2493926_F0001_OB.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0fd/12064104/b36e62b99920/TEMI_A_2493926_F0002_OB.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0fd/12064104/cddacb6a3070/TEMI_A_2493926_F0003_OB.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0fd/12064104/f11acd24e195/TEMI_A_2493926_F0004_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0fd/12064104/552cade627be/TEMI_A_2493926_F0001_OB.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0fd/12064104/b36e62b99920/TEMI_A_2493926_F0002_OB.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0fd/12064104/cddacb6a3070/TEMI_A_2493926_F0003_OB.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0fd/12064104/f11acd24e195/TEMI_A_2493926_F0004_OC.jpg

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本文引用的文献

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血红素通过增强替代途径的激活来干扰补体因子 I 依赖性调节。
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Sialoglycan-binding patterns of bacterial AB toxin B subunits correlate with host range and toxicity, indicating evolution independent of A subunits.细菌 AB 毒素 B 亚基的唾液酸结合模式与宿主范围和毒性相关，表明其与 A 亚基的进化无关。
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Bacterial killing by complement requires membrane attack complex formation via surface-bound C5 convertases.补体通过表面结合的 C5 转化酶形成膜攻击复合物来杀死细菌。
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