期刊
NATURE COMMUNICATIONS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms11567
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资金
- Alfred Osterlunds Foundation
- Edvard Welanders Stiftelse and Finsenstiftelsen
- Hedda and John Forssmans Foundation
- Knut and Alice Wallenberg Foundation
- Thelma Zoegas Foundation
- Royal Physiographic Society
- Swedish Strategic Research Foundation
- Swedish Government Funds for Clinical Research (ALF)
- Swedish Research Council [2012-1883]
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.
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