دورية أكاديمية
أعرض في EDS

An Intracellular Peptidyl-Prolyl cis/trans Isomerase Is Required for Folding and Activity of the Staphylococcus aureus Secreted Virulence Factor Nuclease.

التفاصيل البيبلوغرافية
العنوان: An Intracellular Peptidyl-Prolyl cis/trans Isomerase Is Required for Folding and Activity of the Staphylococcus aureus Secreted Virulence Factor Nuclease.
المؤلفون: Wiemels RE; Department of Biological Sciences, Ohio University, Athens, Ohio, USA., Cech SM; Department of Biological Sciences, Ohio University, Athens, Ohio, USA., Meyer NM; Department of Biological Sciences, Ohio University, Athens, Ohio, USA., Burke CA; Department of Biological Sciences, Ohio University, Athens, Ohio, USA., Weiss A; Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, Florida, USA., Parks AR; Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, Florida, USA., Shaw LN; Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, Florida, USA., Carroll RK; Department of Biological Sciences, Ohio University, Athens, Ohio, USA carrolr3@ohio.edu.
المصدر: Journal of bacteriology [J Bacteriol] 2016 Dec 13; Vol. 199 (1). Date of Electronic Publication: 2016 Dec 13 (Print Publication: 2017).
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural
اللغة: English
بيانات الدورية: Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 2985120R Publication Model: Electronic-Print Cited Medium: Internet ISSN: 1098-5530 (Electronic) Linking ISSN: 00219193 NLM ISO Abbreviation: J Bacteriol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : American Society for Microbiology
مواضيع طبية MeSH: Protein Folding* , Virulence Factors*, Bacterial Proteins/*metabolism , Gene Expression Regulation, Bacterial/*physiology , Peptidylprolyl Isomerase/*metabolism , Staphylococcus aureus/*enzymology, Bacterial Proteins/genetics ; Gene Expression Regulation, Enzymologic/physiology ; Mutation ; Peptidylprolyl Isomerase/genetics ; Staphylococcus aureus/genetics ; Staphylococcus aureus/metabolism
مستخلص: Staphylococcus aureus is an important human pathogen that relies on a large repertoire of secreted and cell wall-associated proteins for pathogenesis. Consequently, the ability of the organism to cause disease is absolutely dependent on its ability to synthesize and successfully secrete these proteins. In this study, we investigate the role of peptidyl-prolyl cis/trans isomerases (PPIases) on the activity of the S. aureus secreted virulence factor nuclease (Nuc). We identify a staphylococcal cyclophilin-type PPIase (PpiB) that is required for optimal activity of Nuc. Disruption of ppiB results in decreased nuclease activity in culture supernatants; however, the levels of Nuc protein are not altered, suggesting that the decrease in activity results from misfolding of Nuc in the absence of PpiB. We go on to demonstrate that PpiB exhibits PPIase activity in vitro, is localized to the bacterial cytosol, and directly interacts with Nuc in vitro to accelerate the rate of Nuc refolding. Finally, we demonstrate an additional role for PpiB in S. aureus hemolysis and demonstrate that the S. aureus parvulin-type PPIase PrsA also plays a role in the activity of secreted virulence factors. The deletion of prsA leads to a decrease in secreted protease and phospholipase activity, similar to that observed in other Gram-positive pathogens. Together, these results demonstrate, for the first time to our knowledge, that PPIases play an important role in the secretion of virulence factors in S. aureus IMPORTANCE: Staphylococcus aureus is a highly dangerous bacterial pathogen capable of causing a variety of infections throughout the human body. The ability of S. aureus to cause disease is largely due to an extensive repertoire of secreted and cell wall-associated proteins, including adhesins, toxins, exoenzymes, and superantigens. These virulence factors, once produced, are typically transported across the cell membrane by the secretory (Sec) system in a denatured state. Consequently, once outside the cell, they must refold into their active form. This step often requires the assistance of bacterial folding proteins, such as PPIases. In this work, we investigate the role of PPIases in S. aureus and uncover a cyclophilin-type enzyme that assists in the folding/refolding of staphylococcal nuclease.
(Copyright © 2016 American Society for Microbiology.)
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معلومات مُعتمدة: R01 AI080626 United States AI NIAID NIH HHS; R21 AI128376 United States AI NIAID NIH HHS
فهرسة مساهمة: Keywords: Nuc; PI-PLC; PPIase; PpiB; PrsA; Staphylococcus aureus; cyclophilin; nuclease; parvulin; protease
المشرفين على المادة: 0 (Bacterial Proteins)
0 (Virulence Factors)
EC 5.2.1.8 (Peptidylprolyl Isomerase)
تواريخ الأحداث: Date Created: 20161101 Date Completed: 20170619 Latest Revision: 20190629
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC5165095
DOI: 10.1128/JB.00453-16
PMID: 27795319
قاعدة البيانات: MEDLINE
الوصف
تدمد:1098-5530
DOI:10.1128/JB.00453-16