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Nat Commun. 2016 May 16;7:11567. doi: 10.1038/ncomms11567.

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

Author information

1
Division of Dermatology and Venereology, Department of Clinical Sciences Lund, Lund University, BMC, Tornavägen 10, Lund SE-22184, Sweden.
2
Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, PO Box 124, Lund SE-22362, Sweden.
3
Division of Infection Medicine, Department of Clinical Sciences Lund, Lund University, BMC, Tornavägen 10, Lund SE-22184, Sweden.
4
Dermatology and Venereology, Skane University Hospital, Lasarettsgatan 15, Lund SE-22185, Sweden.
5
Dermatology, LKCMedicine, Nanyang Technological University, 59 Nanyang Drive, Singapore 636921, Singapore.

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.

PMID:
27181065
PMCID:
PMC4873665
DOI:
10.1038/ncomms11567
[Indexed for MEDLINE]
Free PMC Article

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