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.
Digital Commons Citation
Påhlman, Lisa I.; Marx, Pauline F.; Mörgelin, Matthias; Lukomski, Slawomir; Meijers, Joost C. M.; and Herwald, Heiko, "Thrombin-Activatable Fibrinolysis Inhibitor Binds To Streptococcus Pyogenes By Interacting With Collagen-Like Proteins A And B" (2007). Faculty Scholarship. 709.
Påhlman, Lisa I., Marx, Pauline F., Mörgelin, Matthias., Lukomski, Slawomir., Meijers, Joost C. M., & Herwald, Heiko.(2007). Thrombin-Activatable Fibrinolysis Inhibitor Binds To Streptococcus Pyogenes By Interacting With Collagen-Like Proteins A And B. The Journal Of Biological Chemistry, 282(34), 24873-24881. http://doi.org/10.1074/Jbc.M610015200