Correction: Simultaneous inhibition of two neutrophil serine proteases by the S. aureus innate immune evasion protein EapH2

Le résumé fourni par la source

Simultaneous inhibition of two neutrophil serine proteases by the S. aureus innate immune evasion protein EapH2Journal of Biological ChemistryVol. 299Issue 7PreviewExtracellular adherence protein domain (EAP) proteins are high-affinity, selective inhibitors of neutrophil serine proteases (NSP), including cathepsin-G (CG) and neutrophil elastase (NE). Most Staphylococcus aureus isolates encode for two EAPs, EapH1 and EapH2, that contain a single functional domain and share 43% identity with one another. Although structure/function investigations from our group have shown that EapH1 uses a globally similar binding mode to inhibit CG and NE, NSP inhibition by EapH2 is incompletely understood due to a lack of NSP/EapH2 cocrystal structures. Full-Text PDF Open Access The version of the JBC article entitled “Simultaneous inhibition of two neutrophil serine proteases by the S. aureus innate immune evasion protein EapH2” that published online July 6, 2023 contained several numbering errors in the references. A corrected version of the article posted online on July 25, 2023.

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