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

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

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...

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Bibliographic Details
Main Authors: van der Plas, Mariena J. A., Bhongir, Ravi K. V., Kjellström, Sven, Siller, Helena, Kasetty, Gopinath, Mörgelin, Matthias, Schmidtchen, Artur
Other Authors: Lee Kong Chian School of Medicine (LKCMedicine)
Format: Article
Language:English
Published: 2016
Subjects:
Biological sciences
Microbiology
Immunology
Online Access:https://hdl.handle.net/10356/80660
http://hdl.handle.net/10220/40589
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Institution: Nanyang Technological University
Language: English
Description
Summary: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.

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