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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Evasion of Toll-like receptor 5 by flagellated bacteria
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Evasion of Toll-like receptor 5 by flagellated bacteria

机译：鞭毛细菌对Toll样受体5的逃避

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摘要

Toll-like receptor 5 (TLR5) recognizes an evolutionarily conserved site on bacterial flagellin that is required for flagellar filament assembly and motility. The a and E Proteobacteria, including the important human pathogens Campylobacter jejuni, Helicobacter pylori, and Bartonella bacilliformis, require flagellar motility to efficiently infect mammalian hosts. In this study, we demonstrate that these bacteria make flagellin molecules that are not recognized by TLR5. We map the site responsible for TLR5 evasion to amino acids 89-96 of the N-terminal D1 domain, which is centrally positioned within the previously defined TLRS recognition site. Salmonella flagellin is strongly recognized by TLR5, but mutating residues 89-96 to the corresponding H. pylori flaA sequence abolishes TLR5 recognition and also destroys bacterial motility. To preserve bacterial motility, a and E Proteobacteria possess compensatory amino acid changes in other regions of the flagellin molecule, and we engineer a mutant form of Salmonella flagellin that evades TLR5 but retains motility. These results suggest that TLR5 evasion is critical for the survival of this subset of bacteria at mucosal sites in animals and raise the intriguing possibility that flagellin receptors provided the selective force to drive the evolution of these unique subclasses of bacterial flagellins.
机译：Toll样受体5（TLR5）识别鞭毛细丝组装和运动所需的细菌鞭毛蛋白上的进化保守位点。 a和E变形杆菌，包括重要的人类病原体空肠弯曲菌，幽门螺杆菌和芽孢杆菌，都需要鞭毛运动才能有效感染哺乳动物宿主。在这项研究中，我们证明了这些细菌产生的鞭毛蛋白分子不会被TLR5识别。我们将负责TLR5逃逸的位点映射到N末端D1域的氨基酸89-96，该位点位于先前定义的TLRS识别位点的中央。沙门氏菌鞭毛蛋白可被TLR5强烈识别，但将89-96位残基突变为相应的幽门螺杆菌flaA序列可消除TLR5的识别并破坏细菌的运动能力。为了保持细菌的运动性，a和E变形杆菌在鞭毛蛋白分子的其他区域具有补偿性氨基酸变化，并且我们设计了一种沙门氏菌鞭毛蛋白的突变形式，该突变体可逃避TLR5但保留运动性。这些结果表明，TLR5逃逸对于这种细菌亚群在动物粘膜部位的生存至关重要，并增加了鞭毛蛋白受体提供选择性驱动细菌鞭毛蛋白独特亚类进化的可能性。

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