Document Type


Publication Date



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.

Source Citation

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.



To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.