Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens.

Wizemann, Theresa; Moskovitz, Jackob; Pearce, Barbara J.; Cundell, Diana R.; Arvidson, Cindy Grove; So, Magdalene; Weissbach, Herbert; Brot, Nathan; Masure, H R

doi:10.1073/pnas.93.15.7985

Cited by 132 publications

(156 citation statements)

References 64 publications

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“…Msr enzymes have also been shown to be necessary for host colonization and persistence in Lactobacillus reuteri and H. pylori (Alamuri & Maier, 2004;Walter et al, 2005), which is not only due to protection against oxidative stress but also through a possible role in the maintenance and expression of adhesins, allowing persistence and biofilm formation (Wizemann et al, 1996). Host colonization and persistence studies of the three mutant strains studied here would also shed further light on the in vivo role of MsrA and MsrB from C. jejuni.…”

Section: Discussionmentioning

confidence: 99%

Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni

Atack

Kelly

2008

Microbiology

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The microaerophilic food-borne pathogen Campylobacter jejuni is exposed to highly variable oxygen concentrations during its life cycle and employs a variety of protection mechanisms to resist oxidative stress. However, not all of the enzymes that mediate such protection have yet been identified. Two genes in strain NCTC 11168, Cj0637c and Cj1112c, are predicted to encode unrelated methionine sulphoxide reductases, which may repair oxidized methionine residues in proteins and thus contribute to oxidative stress defence. Cj0637 and Cj1112 were overexpressed, purified and shown by a coupled thioredoxin-thioredoxin reductase-NADPH assay to catalyse the stereospecific reduction of the S and R diastereoisomers, respectively, of the model compound methyl p-tolyl sulphoxide. Cj0637 is thus identified as MsrA and Cj1112 as MsrB. The contribution of these enzymes to oxidative and nitrosative stress resistance in C. jejuni was assessed by phenotypic analysis of a set of isogenic msrA, msrB and msrA/B insertion mutants. As RT-PCR data suggested a polar effect on Cj1111c in the msrB mutant, an msrB/ msrB + merodiploid complementation strain was also constructed. The msrA/B strain was severely growth inhibited under standard microaerobic conditions, whereas the msrA and msrB strains grew normally. Agar plate disc diffusion assays showed that all mutants displayed increased sensitivity to hydrogen peroxide, organic peroxide, superoxide, and nitrosative and disulphide stress, but quantitative cell viability assays showed that the msrA/B double mutant was markedly more sensitive to both oxidative and nitrosative stress. All of the stress-sensitivity phenotypes observed for the msrB mutant were restored to wild-type in the msrB/msrB + merodiploid. It is concluded that MsrA and MsrB make a significant contribution to the protection of C. jejuni against oxidative and nitrosative stress.

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Section: Discussionmentioning

confidence: 99%

Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni

Atack

Kelly

2008

Microbiology

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“…Both MsrA and MsrB have been shown to play a role in the oxidative stress response and pathogenicity of microorganisms. For example, a decrease in infectivity of Streptococcus pneumoniae has been observed after the deletion of the msrAB1 gene (33). Similarly, a study on the pathogenic actinomycete Mycobacterium tuberculosis, which can survive major reactive oxygen species and reactive nitrogen species attacks during the host immune response within macrophages, has shown that MsrA and MsrB single and double deletion strains were sensitive for oxidative stress (34).…”

Section: Discussionmentioning

confidence: 99%

Corynebacterium diphtheriae Methionine Sulfoxide Reductase A Exploits a Unique Mycothiol Redox Relay Mechanism

Tossounian

Pedre

Wahni

et al. 2015

Journal of Biological Chemistry

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Background: Methionine sulfoxide post-translational modifications have an important new signaling role in cells. Results: Methionine sulfoxide reductase MsrA of the pathogenic actinomycete Corynebacterium diphtheriae (Cd-MsrA) uses a unique intramolecular redox relay mechanism coupled to mycothiol. Conclusion: For methionine sulfoxide control, Cd-MsrA is flexible in receiving electrons from both the thioredoxin and the mycothiol pathways. Significance: C. diphtheriae MsrA is a redox regulator for methionine sulfoxide signaling.

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“…This suggested that the CBPs bound to receptors on the human cells and thereby prevented CBP-mediated bacterial attachment. The demonstration of a direct CBPhuman cell interaction that leads to a loss of adherence distinguishes the CBPs from other pneumococcal proteins, such as the peptide permeases, PlpA (Cundell et al, 1995a), AmiA (Cundell et al, 1995a), a pyruvate oxidase (SpxB) (Spellerberg et al, 1996) and the peptide methionine sulphoxide reductase (MsrA) (Wizemann et al, 1996), which have been identified in genetic studies as affecting bacterial adherence. Although loss of these elements decreases the capacity of the bacteria to adhere, there was no direct evidence that they exhibited competitive inhibition of adherence, a key characteristic of a structural adhesin.…”

Section: Discussionmentioning

confidence: 99%

Contribution of novel choline‐binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae

Rosenow

Ryan

Weiser

et al. 1997

Molecular Microbiology

438

465

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SummaryThe surface of Streptococcus pneumoniae is decorated with a family of choline-binding proteins (CBPs) that are non-covalently bound to the phosphorylcholine of the teichoic acid. Two examples (PspA, a protective antigen, and LytA, the major autolysin) have been well characterized. We identified additional CPBs and characterized a new CBP, CbpA, as an adhesin and a determinant of virulence. Using choline immobilized on a solid matrix, a mixture of proteins from a pspA-deficient strain of pneumococcus was eluted in a choline-dependent fashion. Antisera to these proteins passively protected mice challenged in the peritoneum with a lethal dose of pneumococci. The predominant component of this mixture, CbpA, is a 75-kDa surface-exposed protein that reacts with human convalescent antisera. The deduced sequence from the corresponding gene showed a chimeric architecture with a unique N-terminal region and a C-terminal domain consisting of 10 repeated choline-binding domains nearly identical to PspA. A cbpA-deficient mutant showed a >50% reduction in adherence to cytokine-activated human cells and failed to bind to immobilized sialic acid or lacto-N-neotetraose, known pneumococcal ligands on eukaryotic cells. Carriage of this mutant in an animal model of nasopharyngeal colonization was reduced 100-fold. There was no difference between the parent strain and this mutant in an intraperitoneal model of sepsis. These data for CbpA extend the important functions of the CBP family to bacterial adherence and identify a pneumococcal vaccine candidate.

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Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens.

Cited by 132 publications

References 64 publications

Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni

Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni

Corynebacterium diphtheriae Methionine Sulfoxide Reductase A Exploits a Unique Mycothiol Redox Relay Mechanism

Contribution of novel choline‐binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae

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