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Thrombin activatable fibrinolysis inhibitor binds to Streptococcus pyogenes by interacting with collagen-like surface proteins A and B.

Påhlman, Lisa LU ; Marx, Pauline F; Mörgelin, Matthias LU ; Lukomski, Slawomir; Meijers, Joost C M and Herwald, Heiko LU (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)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
282
issue
34
pages
24873 - 24881
publisher
ASBMB
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
2007-12-19 11:14:35
date last changed
2017-09-10 03:31:41
@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    = {ASBMB},
  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          = {http://dx.doi.org/10.1074/jbc.M610015200},
  volume       = {282},
  year         = {2007},
}