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Staphylococcus aureus secretes a unique class of neutrophil serine protease inhibitors

Stapels, Daphne A. C., Ramyar, Kasra X., Bischoff, Markus, von Köckritz-Blickwede, Maren, Milder, Fin J., Ruyken, Maartje, Eisenbeis, Janina, McWhorter, William J., Herrmann, Mathias, van Kessel, Kok P. M., Geisbrecht, Brian V., Rooijakkers, Suzan H. M.
Proceedings of the National Academy of Sciences of the United States of America 2014 v.111 no.36 pp. 13187-13192
Staphylococcus aureus, bacteria, crystallography, immune response, neutrophils, pathogenicity, proteinase inhibitors, proteins, serine proteinases
Significance Neutrophils are among the first immune cells to migrate to the site of infection and clear invading bacteria. They store large amounts of neutrophil serine proteases (NSPs) that play key roles in immune defense. Unfortunately, NSPs also contribute to tissue destruction in a variety of inflammatory disorders. In this study we discover that the pathogenic bacterium Staphylococcus aureus secretes a family of highly potent and specific NSP inhibitors that promote the pathogenicity of this bacterium in vivo. From crystallography experiments, we conclude that these proteins constitute a unique class of NSP inhibitors, which can be used to design novel treatment strategies against excessive NSP activity. Furthermore, this study significantly increases our understanding of the complex nature of S. aureus infections.