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

van der Plas MJ, Bhongir RK, Kjellström S, Siller H, Kasetty G, Mörgelin M, Schmidtchen A

Nat Commun 7 (-) 11567 [2016-05-16; online 2016-05-16]

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.

Targeted and Structural Proteomics [Service]

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PubMed 27181065

DOI 10.1038/ncomms11567

Crossref 10.1038/ncomms11567

ncomms11567

pmc PMC4873665