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

Mariena J. A. van der Plas (), Ravi K. V. Bhongir, Sven Kjellström, Helena Siller, Gopinath Kasetty, Matthias Mörgelin and Artur Schmidtchen
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Mariena J. A. van der Plas: Lund University, BMC
Ravi K. V. Bhongir: Lund University, BMC
Sven Kjellström: Center for Molecular Protein Science, Lund University
Helena Siller: Lund University, BMC
Gopinath Kasetty: Lund University, BMC
Matthias Mörgelin: Lund University, BMC
Artur Schmidtchen: Lund University, BMC

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms11567

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