Crystal Structure of Staphopain C from Staphylococcus aureus

Malgorzata Magoch; Alastair G McEwen; Valeria Napolitano; Benedykt Władyka; Grzegorz Dubin

doi:10.3390/molecules28114407

Crystal Structure of Staphopain C from Staphylococcus aureus

Molecules. 2023 May 29;28(11):4407. doi: 10.3390/molecules28114407.

Authors

Malgorzata Magoch^{1

2}, Alastair G McEwen³, Valeria Napolitano^{1

2}, Benedykt Władyka², Grzegorz Dubin¹

Affiliations

¹ Malopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland.
² Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-387 Krakow, Poland.
³ CNRS, INSERM, Université de Strasbourg, IGBMC UMR 7104-UMR-S 1258, F-67400 Illkirch, France.

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

Bacterial Proteins / chemistry
Cysteine Proteases* / metabolism
Humans
Papain / metabolism
Staphylococcal Infections* / microbiology
Staphylococcus aureus
Virulence Factors / metabolism

Substances

Cysteine Proteases
Papain
Virulence Factors
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.