Journal
CHEMISTRY & BIOLOGY
Volume 15, Issue 9, Pages 960-968Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2008.07.021
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Funding
- Swedish Research Council [14800, 14767, 09915]
- Commission of the European Communities
- Royal Physiographic Society in Lund
- Faculty of Medicine at Lund University
- Insamlingsstiftelsen at Umea University
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Human cystatin C is considered the physiologically most important inhibitor of endogenous papain-like cysteine proteases. We present here an unexpected function of cystatin C. Instead of acting as an inhibitor, cystatin C acts as a facultative, endogenous cofactor for the papain-like IgG-cleaving enzyme IdeS of the human pathogen Streptococcus pyogenes. IdeS activity is not dependent on cystatin C, but is significantly enhanced in the presence of cystatin C. We report a protease inhibitor that accelerates the activity of its putative target protease and a unique example of how a host protease inhibitor is hijacked by a bacterial protease to increase its activity. This finding has important implications for the view on protease-inhibitor interactions, and is relevant to consider in the therapeutic use of protease inhibitors.
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