Pseudomonas aeruginosa elastase cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses
(2016) In Nature Communications 7.- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/f126110c-7c6e-44ef-a75d-4fbf58f0d71d
- author
- van Der Plas, Mariena
LU
; Bhongir, Ravi
LU
; Kjellström, Sven LU ; Siller, Helena ; Kasetty, Gopinath LU ; Mörgelin, Matthias LU and Schmidtchen, Artur LU
- organization
- publishing date
- 2016-05-16
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- inflammatory responses, Pseudomonas aeruginosa
- in
- Nature Communications
- volume
- 7
- article number
- 11567
- pages
- 13 pages
- publisher
- Nature Publishing Group
- external identifiers
-
- scopus:84968883567
- pmid:27181065
- wos:000375938800001
- ISSN
- 2041-1723
- DOI
- 10.1038/ncomms11567
- project
- Host-pathogen interactions and the development of chronic infections
- language
- English
- LU publication?
- yes
- id
- f126110c-7c6e-44ef-a75d-4fbf58f0d71d
- date added to LUP
- 2016-06-16 08:53:45
- date last changed
- 2025-01-12 07:17:09
@article{f126110c-7c6e-44ef-a75d-4fbf58f0d71d, abstract = {{<p>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.</p>}}, author = {{van Der Plas, Mariena and Bhongir, Ravi and Kjellström, Sven and Siller, Helena and Kasetty, Gopinath and Mörgelin, Matthias and Schmidtchen, Artur}}, issn = {{2041-1723}}, keywords = {{inflammatory responses; Pseudomonas aeruginosa}}, language = {{eng}}, month = {{05}}, publisher = {{Nature Publishing Group}}, series = {{Nature Communications}}, title = {{<i>Pseudomonas aeruginosa</i> elastase cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses}}, url = {{http://dx.doi.org/10.1038/ncomms11567}}, doi = {{10.1038/ncomms11567}}, volume = {{7}}, year = {{2016}}, }