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Abstract
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.
Original language | English |
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Article number | 11567 |
Number of pages | 13 |
Journal | Nature Communications |
Volume | 7 |
DOIs | |
Publication status | Published - 2016 May 16 |
Subject classification (UKÄ)
- Infectious Medicine
Free keywords
- inflammatory responses
- Pseudomonas aeruginosa
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Host-pathogen interactions and the development of chronic infections
van Der Plas, M. (PI)
2010/12/01 → …
Project: Research