Division of Dermatology and Venereology, Department of Clinical Sciences Lund, Lund University, BMC, Tornavägen 10, Lund SE-22184, Sweden.
Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, PO Box 124, Lund SE-22362, Sweden.
Nat Commun. 2016 May 16;7:11567. doi: 10.1038/ncomms11567.
Pseudomonas aeruginosa is an opportunistic pathogen known for its immune evasive abilities amongst others by degradation of a large variety of host proteins. Here we show that digestion of thrombin by P. aeruginosa elastase leads to the release of the C-terminal thrombin-derived peptide FYT21, which inhibits pro-inflammatory responses to several pathogen-associated molecular patterns in vitro and in vivo by preventing toll-like receptor dimerization and subsequent activation of down-stream signalling pathways. Thus, P. aeruginosa 'hijacks' an endogenous anti-inflammatory peptide-based mechanism, thereby enabling modulation and circumvention of host responses.
铜绿假单胞菌是一种机会性病原体，以其免疫逃避能力而闻名，其中包括降解多种宿主蛋白。在这里，我们表明，铜绿假单胞菌弹性蛋白酶对凝血酶的消化导致释放凝血酶衍生的 C 端肽 FYT21，该肽在体外和体内通过防止 Toll 样受体二聚化和随后的下游信号通路激活来抑制几种病原体相关分子模式的促炎反应。因此，铜绿假单胞菌“劫持”了一种内源性基于抗炎肽的机制，从而能够调节和规避宿主反应。
