Pseudomonas aeruginosa elastase cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses

Research output: Contribution to journalArticle


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.


External organisations
  • Nanyang Technological University
  • Lund University
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Infectious Medicine


  • inflammatory responses, Pseudomonas aeruginosa
Original languageEnglish
Article number11567
Number of pages13
JournalNature Communications
Publication statusPublished - 2016 May 16
Publication categoryResearch

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