Identification of peptidic inhibitors of the alternative complement pathway based on Staphylococcus aureus SCIN proteins.

ABSTRACT: The complement system plays a central role in a number of human inflammatory diseases, and there is a significant need for development of complement-directed therapies. The discovery of an arsenal of anti-complement proteins secreted by the pathogen Staphylococcus aureus brought with it the potential for harnessing the powerful inhibitory properties of these molecules. One such family of inhibitors, the SCINs, interact with a functional "hot-spot" on the surface of C3b. SCINs not only stabilize an inactive form of the alternative pathway (AP) C3 convertase (C3bBb), but also overlap the C3b binding site of complement factors B and H. Here we determined that a conserved Arg residue in SCINs is critical for function of full-length SCIN proteins. Despite this, we also found SCIN-specific diffe

SUBMITTER: Summers BJ 

PROVIDER: S-EPMC4565748 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature