Thrombin activatable fibrinolysis inhibitor binds to Streptococcus pyogenes by interacting with collagen-like surface proteins A and B.
(2007) In Journal of Biological Chemistry 282(34). p.24873-24881- Abstract
- Regulation of proteolysis is a critical element of the host immune system and plays an important role in the induction of pro- and anti-inflammatory reactions in response to infection. Some bacterial species take advantage of these processes and recruit host proteinases to their surface in order to counteract the host attack. Here we show that Thrombin-activatable Fibrinolysis Inhibitor (TAFI), a zinc-dependent procarboxypeptidase, binds to the surface of group A streptococci of an M41 serotype. The interaction is mediated by the streptococcal collagen-like surface proteins A and B (Sc1A and Sc1B), and the streptococcal-associated TAFI is then processed at the bacterial surface via plasmin and thrombin-thrombomodulin. These findings... (More)
- Regulation of proteolysis is a critical element of the host immune system and plays an important role in the induction of pro- and anti-inflammatory reactions in response to infection. Some bacterial species take advantage of these processes and recruit host proteinases to their surface in order to counteract the host attack. Here we show that Thrombin-activatable Fibrinolysis Inhibitor (TAFI), a zinc-dependent procarboxypeptidase, binds to the surface of group A streptococci of an M41 serotype. The interaction is mediated by the streptococcal collagen-like surface proteins A and B (Sc1A and Sc1B), and the streptococcal-associated TAFI is then processed at the bacterial surface via plasmin and thrombin-thrombomodulin. These findings suggest an important role for TAFI in the modulation of host responses by streptococci. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/539921
- author
- Påhlman, Lisa LU ; Marx, Pauline F ; Mörgelin, Matthias LU ; Lukomski, Slawomir ; Meijers, Joost C M and Herwald, Heiko LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 282
- issue
- 34
- pages
- 24873 - 24881
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000248933000044
- scopus:34548307247
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M610015200
- language
- English
- LU publication?
- yes
- id
- e3688a92-93a7-4bdf-8c96-c4e14e9d7f78 (old id 539921)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17553807&dopt=Abstract
- date added to LUP
- 2016-04-01 11:38:02
- date last changed
- 2022-01-26 07:54:20
@article{e3688a92-93a7-4bdf-8c96-c4e14e9d7f78, abstract = {{Regulation of proteolysis is a critical element of the host immune system and plays an important role in the induction of pro- and anti-inflammatory reactions in response to infection. Some bacterial species take advantage of these processes and recruit host proteinases to their surface in order to counteract the host attack. Here we show that Thrombin-activatable Fibrinolysis Inhibitor (TAFI), a zinc-dependent procarboxypeptidase, binds to the surface of group A streptococci of an M41 serotype. The interaction is mediated by the streptococcal collagen-like surface proteins A and B (Sc1A and Sc1B), and the streptococcal-associated TAFI is then processed at the bacterial surface via plasmin and thrombin-thrombomodulin. These findings suggest an important role for TAFI in the modulation of host responses by streptococci.}}, author = {{Påhlman, Lisa and Marx, Pauline F and Mörgelin, Matthias and Lukomski, Slawomir and Meijers, Joost C M and Herwald, Heiko}}, issn = {{1083-351X}}, language = {{eng}}, number = {{34}}, pages = {{24873--24881}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{Thrombin activatable fibrinolysis inhibitor binds to Streptococcus pyogenes by interacting with collagen-like surface proteins A and B.}}, url = {{https://lup.lub.lu.se/search/files/2570783/626021.pdf}}, doi = {{10.1074/jbc.M610015200}}, volume = {{282}}, year = {{2007}}, }