Methionine sulfoxide reductase A (MsrA) contributes to Salmonella Typhimurium survival against oxidative attack of neutrophils

Trivedi, Raj Narayan; Agarwal, Priti; Kumawat, Manoj; Pesingi, Pavan Kumar; Gupta, Vivek Kumar; Goswami, T. K.; Mahawar, Manish

doi:10.1016/j.imbio.2015.07.011

Cited by 20 publications

(9 citation statements)

References 32 publications

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“…Oxidation of methionine residues of acid-soluble spore proteins, (SASP), in MSRA-deficient cells of B. subtilis reduces their ability to bind DNA, which is significant for the long-term survival of spores [ 52 ]. MSRA-deficient S. Typhimurium showed normal growth in broth but was sensitive to HOCl [ 53 ]. Lack of MSRAB2 in Streptococcus pneumoniae enhanced its killing by H 2 O 2 [ 54 ].…”

Section: Defense From Oxidantsmentioning

confidence: 99%

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

Singh

Baum

2018

Antioxidants

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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.

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Section: Defense From Oxidantsmentioning

confidence: 99%

“…These MSRA1-deficient cells also showed a decrease in survival in mouse tissue when compared with wild-type S. aureus [ 13 ]. Further, reduced MSRA activity in many bacteria impacted survival inside phagocytic cells [ 47 , 53 , 58 , 59 ].…”

Section: Methionine Sulfoxide Reductases and Virulencementioning

confidence: 99%

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

Singh

Baum

2018

Antioxidants

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“…Similar results were observed for MPO in the serum of SA+ mice. The higher concentration of MPO observed in SA+ mice can be directly associated with S. Typhimurium infection, since this enzyme produces hypochlorous acid (HOCl), a key cytotoxic antimicrobial product released by neutrophils against the pathogen [52]. Additionally, the higher concentration of both KC and MPO observed in the intestine at 48 hpi likely correlates to the higher infiltration of neutrophils observed at this time point.…”

Section: Mcramp Deficiency Modifies the Host Immune Responsementioning

confidence: 97%

The absence of murine cathelicidin-related antimicrobial peptide impacts host responses enhancing Salmonella enterica serovar Typhimurium infection

et al. 2020

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Background Cathelicidins are a class of antimicrobial peptide, and the murine cathelicidin-related antimicrobial peptide (mCRAMP) has been demonstrated in vitro to impair Salmonella enterica serovar Typhimurium proliferation. However, the impact of mCRAMP on host responses and the microbiota following S. Typhimurium infection has not been determined. In this study mCRAMP−/− and mCRAMP+/+ mice (± streptomycin) were orally inoculated with S. enterica serovar Typhimurium DT104 (SA +), and impacts on the host and enteric bacterial communities were temporally evaluated. Results Higher densities of the pathogen were observed in cecal digesta and associated with mucosa in SA+/mCRAMP−/− mice that were pretreated (ST+) and not pretreated (ST−) with streptomycin at 24 h post-inoculation (hpi). Both SA+/ST+/mCRAMP−/− and SA+/ST−/mCRAMP−/− mice were more susceptible to infection exhibiting greater histopathologic changes (e.g. epithelial injury, leukocyte infiltration, goblet cell loss) at 48 hpi. Correspondingly, immune responses in SA+/ST+/mCRAMP–/− and SA+/ST−/mCRAMP–/− mice were affected (e.g. Ifnγ, Kc, Inos, Il1β, RegIIIγ). Systemic dissemination of the pathogen was characterized by metabolomics, and the liver metabolome was affected to a greater degree in SA+/ST+/mCRAMP–/− and SA+/ST−/mCRAMP–/− mice (e.g. taurine, cadaverine). Treatment-specific changes to the structure of the enteric microbiota were associated with infection and mCRAMP deficiency, with a higher abundance of Enterobacteriaceae and Veillonellaceae observed in infected null mice. The microbiota of mice that were administered the antibiotic and infected with Salmonella was dominated by Proteobacteria. Conclusion The study findings showed that the absence of mCRAMP modulated both host responses and the enteric microbiota enhancing local and systemic infection by Salmonella Typhimurium.

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“…All the three are present in cytoplasmic compartment. MsrA repairs protein-bound as well as free Met-SO and is essential for the survival of this bacterium under oxidative stress (Denkel et al 2011;Trivedi et al 2015). MsrB repairs protein-bound Met-SO though it is dispensable for stress survival of this bacterium (Denkel et al 2011).…”

Section: Msrs In Salmonellamentioning

confidence: 99%

Role of protein repair enzymes in oxidative stress survival and virulence of Salmonella

et al. 2020

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Purpose Proteins are the principal biomolecules in bacteria that are affected by the oxidants produced by the phagocytic cells. Most of the protein damage is irreparable though few unfolded proteins and covalently modified amino acids can be repaired by chaperones and repair enzymes respectively. This study reviews the three protein repair enzymes, protein l-isoaspartyl O-methyl transferase (PIMT), peptidyl proline cis-trans isomerase (PPIase), and methionine sulfoxide reductase (MSR). Methods Published articles regarding protein repair enzymes were collected from Google Scholar and PubMed. The information obtained from the research articles was analyzed and categorized into general information about the enzyme, mechanism of action, and role played by the enzymes in bacteria. Special emphasis was given to the importance of these enzymes in Salmonella Typhimurium. Results Protein repair is the direct and energetically preferred way of replenishing the cellular protein pool without translational synthesis. Under the oxidative stress mounted by the host during the infection, protein repair becomes very crucial for the survival of the bacterial pathogens. Only a few covalent modifications of amino acids are reversible by the protein repair enzymes, and they are highly specific in activity. Deletion mutants of these enzymes in different bacteria revealed their importance in the virulence and oxidative stress survival. Conclusion PIMT repairs isoaspartate residues, PPiase catalyzes the conversion of cis-trans forms of proline residues, while MSR repairs oxidized methionine (Met) residues in the proteins. These repair enzymes maintain the activities of the target protein(s), thus aid in bacterial survival and virulence. The interventions which can interfere with this mechanism could be used for the development of novel therapeutics.

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Methionine sulfoxide reductase A (MsrA) contributes to Salmonella Typhimurium survival against oxidative attack of neutrophils

Cited by 20 publications

References 32 publications

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

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

The absence of murine cathelicidin-related antimicrobial peptide impacts host responses enhancing Salmonella enterica serovar Typhimurium infection

Role of protein repair enzymes in oxidative stress survival and virulence of Salmonella

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