Abstract
Staphylococcus aureus is a common opportunistic pathogen of humans and livestock that causes a wide variety of infections. The success of S. aureus as a pathogen depends on the production of an array of virulence factors including cysteine proteases (staphopains)-major secreted proteases of certain strains of the bacterium. Here, we report the three-dimensional structure of staphopain C (ScpA2) of S. aureus, which shows the typical papain-like fold and uncovers a detailed molecular description of the active site. Because the protein is involved in the pathogenesis of a chicken disease, our work provides the foundation for inhibitor design and potential antimicrobial strategies against this pathogen.
Keywords:
ScpA2; Staphylococcus aureus; X-ray crystallography; cysteine protease; staphopain; virulence factor.
MeSH terms
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Bacterial Proteins / chemistry
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Cysteine Proteases* / metabolism
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Humans
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Papain / metabolism
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Staphylococcal Infections* / microbiology
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Staphylococcus aureus
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Virulence Factors / metabolism
Substances
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Cysteine Proteases
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Papain
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Virulence Factors
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Bacterial Proteins
Grants and funding
This work was supported, in part, by grants UMO-2011/01/D/NZ1/01169 (to G.D.) and N N303 813340 (to B.W.) from the Polish National Science Centre. This work of the Interdisciplinary Thematic Institute IMCBio, as part of the ITI 2021-2028 program of the University of Strasbourg, CNRS and Inserm, was supported by IdEx Unistra (ANR-10-IDEX-0002); by the SFRI-STRAT’US project (ANR 20-SFRI-0012) and EUR IMCBio (ANR-17-EURE-0023) under the framework of the French Investments for the Future Program; and by French Infrastructure for Integrated Structural Biology (FRISBI) AND-10-INSB-005 and Instruct-ERIC.