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J. Biol. Chem., Vol. 282, Issue 34, 24873-24881, August 24, 2007

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Thrombin-activatable Fibrinolysis Inhibitor Binds to Streptococcus pyogenes by Interacting with Collagen-like Proteins A and B^*

Lisa I. Påhlman¹, Pauline F. Marx, Matthias Mörgelin, Slawomir Lukomski^¶, Joost C. M. Meijers, and Heiko Herwald

From the Department of Clinical Sciences, Section for Clinical and Experimental Infection Medicine, Lund University, SE-22184 Lund, Sweden, Departments of Vascular and Experimental Vascular Medicine, Academic Medical Center, 1100 DD Amsterdam, The Netherlands, and ^¶Department of Microbiology, Immunology, and Cell Biology, West Virginia University School of Medicine, Morgantown, West Virginia 26506

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 (SclA and SclB), 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.

Received for publication, October 25, 2006 , and in revised form, June 5, 2007.

^* This work was supported in part by the foundation of Åke Wiberg, Alfred Österlund, Crafoord, Tore Nilson, Greta and Johan Kock, the Swedish Foundation for Strategic Research, King Gustaf V's 80-years Fund, the Royal Physiographical Society in Lund, the Medical Faculty of Lund University, the Swedish Research Council (Projects 13413 and 7480), Hansa Medical AB, a VENI grant from the Netherlands Organization for Scientific Research (NWO Grant 916.36.104) (to P. F. M.), and National Institutes of Health Grant AI50666 (to S. L.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBank^TM/EBI Data Bank with accession number(s) EF042101 and EF042102.

¹ To whom correspondence should be addressed: Dept. of Clinical Sciences, Section for Clinical and Experimental Infection Medicine, BMC B14, Lund University, Tornavägen 10, SE-221 84 Lund, Sweden. Tel.: 46-46-2228592; Fax: 46-46-157756; E-mail: Lisa.Pahlman{at}med.lu.se.

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