The Role of Methionine Sulfoxide Reductases in Oxidative Stress Tolerance and Virulence of Staphylococcus aureus and Other Bacteria

Vineet K Singh¹, Kuldeep Singh², Kyle Baum³

Affiliations

¹ Department of Microbiology and Immunology, A.T. Still University of Health Sciences, Kirksville, MO 63501, USA. vsingh@atsu.edu.
² Mayo Clinic, Rochester, MN 53905, USA. singh.kuldeep@mayo.edu.
³ Department of Microbiology and Immunology, A.T. Still University of Health Sciences, Kirksville, MO 63501, USA. krbaum@atsu.edu.

PMID: 30274148
PMCID: PMC6210949
DOI: 10.3390/antiox7100128

Review

The Role of Methionine Sulfoxide Reductases in Oxidative Stress Tolerance and Virulence of Staphylococcus aureus and Other Bacteria

Vineet K Singh et al. Antioxidants (Basel). 2018.

. 2018 Sep 28;7(10):128.

doi: 10.3390/antiox7100128.

Authors

Vineet K Singh¹, Kuldeep Singh², Kyle Baum³

Affiliations

¹ Department of Microbiology and Immunology, A.T. Still University of Health Sciences, Kirksville, MO 63501, USA. vsingh@atsu.edu.
² Mayo Clinic, Rochester, MN 53905, USA. singh.kuldeep@mayo.edu.
³ Department of Microbiology and Immunology, A.T. Still University of Health Sciences, Kirksville, MO 63501, USA. krbaum@atsu.edu.

PMID: 30274148
PMCID: PMC6210949
DOI: 10.3390/antiox7100128

Abstract

Methionine sulfoxide reductases (MSRA1 and MSRB) are proteins overproduced in Staphylococcus aureus during exposure with cell wall-active antibiotics. Later studies identified the presence of two additional MSRA proteins (MSRA2 and MSRA3) in S. aureus. These MSR proteins have been characterized in many other bacteria as well. This review provides the current knowledge about the conditions and regulatory network that mimic the expression of these MSR encoding genes and their role in defense from oxidative stress and virulence.

Keywords: MSRA; MSRB; oxidative stress; virulence.

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Conflict of interest statement

These authors declare no conflict of interest.

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References

1. Achilli C., Ciana A., Minetti G. The discovery of methionine sulfoxide reductase enzymes: An historical account and future perspectives. Biofactors. 2015;41:135–152. doi: 10.1002/biof.1214. - DOI - PubMed
1. Vogt W. Oxidation of methionyl residues in proteins: Tools, targets, and reversal. Free Radic. Biol. Med. 1995;18:93–105. doi: 10.1016/0891-5849(94)00158-G. - DOI - PubMed
1. Abrams W.R., Weinbaum G., Weissbach L., Weissbach H., Brot B. Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity. Proc. Natl. Acad. Sci. USA. 1981;78:7483–7486. doi: 10.1073/pnas.78.12.7483. - DOI - PMC - PubMed
1. Brot N., Weissbach L., Werth J., Weissbach H. Enzymatic reduction of protein-bound methionine sulfoxide. Proc. Natl. Acad. Sci. USA. 1981;78:2155–2158. doi: 10.1073/pnas.78.4.2155. - DOI - PMC - PubMed
1. Brot N., Weissbach H. Peptide methionine sulfoxide reductase: Biochemistry and physiological role. Biopolymers. 2000;55:288–296. doi: 10.1002/1097-0282(2000)55:4<288::AID-BIP1002>3.0.CO;2-M. - DOI - PubMed

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The Role of Methionine Sulfoxide Reductases in Oxidative Stress Tolerance and Virulence of Staphylococcus aureus and Other Bacteria

Affiliations

The Role of Methionine Sulfoxide Reductases in Oxidative Stress Tolerance and Virulence of Staphylococcus aureus and Other Bacteria

Authors

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Abstract

Conflict of interest statement

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