A peroxiredoxin from Mycoplasma hyopneumoniae with a possible role in H2O2 detoxification

Machado, Claudio Xavier; Pinto, Paulo Marcos; Zaha, Arnaldo; Ferreira, Henrique Bunselmeyer

doi:10.1099/mic.0.030643-0

Cited by 15 publications

(4 citation statements)

References 39 publications

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“…The number of P97 and P146 pI isoforms observed in these strains was also distinct, which denotes differences in post-translational processing. Two proteins were identified that showed overexpression in the J strain: 1) P216, an adhesin; and thiol peroxidase (TPx, reannotated as a peroxiredoxin [18]), an oxidative stress-related protein described as a virulence factor for other pathogenic bacteria [19,20]. …”

Section: Resultsmentioning

confidence: 99%

Comparative proteomic analysis of pathogenic and non-pathogenic strains from the swine pathogen Mycoplasma hyopneumoniae

et al. 2009

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BackgroundMycoplasma hyopneumoniae is a highly infectious swine pathogen and is the causative agent of enzootic pneumonia (EP). Following the previous report of a proteomic survey of the pathogenic 7448 strain of swine pathogen, Mycoplasma hyopneumoniae, we performed comparative protein profiling of three M. hyopneumoniae strains, namely the non-pathogenic J strain and the two pathogenic strains 7448 and 7422.ResultsIn 2DE comparisons, we were able to identify differences in expression levels for 67 proteins, including the overexpression of some cytoadherence-related proteins only in the pathogenic strains. 2DE immunoblot analyses allowed the identification of differential proteolytic cleavage patterns of the P97 adhesin in the three strains. For more comprehensive protein profiling, an LC-MS/MS strategy was used. Overall, 35% of the M. hyopneumoniae genome coding capacity was covered. Partially overlapping profiles of identified proteins were observed in the strains with 81 proteins identified only in one strain and 54 proteins identified in two strains. Abundance analysis of proteins detected in more than one strain demonstrates the relative overexpression of 64 proteins, including the P97 adhesin in the pathogenic strains.ConclusionsOur results indicate the physiological differences between the non-pathogenic strain, with its non-infective proliferate lifestyle, and the pathogenic strains, with its constitutive expression of adhesins, which would render the bacterium competent for adhesion and infection prior to host contact.

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Section: Resultsmentioning

confidence: 99%

Comparative proteomic analysis of pathogenic and non-pathogenic strains from the swine pathogen Mycoplasma hyopneumoniae

et al. 2009

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“…In the absence of H 2 O 2 -degrading enzymes in mycoplasmas, such as catalase or superoxide dismutase, H 2 O 2 could potentially diffuse freely outside of the mycoplasma cells even if its diffusion is known to be limited (Bienert et al, 2007). A peroxiredoxin, belonging to a family of antioxidant enzymes (EC 1.11.1.15) able to reduce H 2 O 2 , was identified in Mycoplasma hyopneumoniae (Machado et al, 2009). Orthologs have been identified in other mycoplasmas, including species of the “ Mycoplasma mycoides cluster” such as Mmc strain GM12 (MMCAP2_0054), Mmc strain 95010 (MLC_0500), Mmm strain PG1 (MSC_0053), but no precise function in cell detoxification has been proposed in these organisms.…”

Section: Discussionmentioning

confidence: 99%

Evidence for the Cytoplasmic Localization of the L-α-Glycerophosphate Oxidase in Members of the “Mycoplasma mycoides Cluster”

et al. 2019

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Members of the “ Mycoplasma mycoides cluster” are important animal pathogens causing diseases including contagious bovine pleuropneumonia and contagious caprine pleuropneumonia, which are of utmost importance in Africa or Asia. Even if all existing vaccines have shortcomings, vaccination of herds is still considered the best way to fight mycoplasma diseases, especially with the recent and dramatic increase of antimicrobial resistance observed in many mycoplasma species. A new generation of vaccines will benefit from a better understanding of the pathogenesis of mycoplasmas, which is very patchy up to now. In particular, surface-exposed virulence traits are likely to induce a protective immune response when formulated in a vaccine. The candidate virulence factor L-α-glycerophosphate oxidase (GlpO), shared by many mycoplasmas including Mycoplasma pneumoniae , was suggested to be a surface-exposed enzyme in Mycoplasma mycoides subsp. mycoides responsible for the production of hydrogen peroxide directly into the host cells. We produced a glpO isogenic mutant GM12::YCpMmyc1.1- ΔglpO using in-yeast synthetic genomics tools including the tandem-repeat endonuclease cleavage (TREC) technique followed by the back-transplantation of the engineered genome into a mycoplasma recipient cell. GlpO localization in the mutant and its parental strain was assessed using scanning electron microscopy (SEM). We obtained conflicting results and this led us to re-evaluate the localization of GlpO using a combination of in silico and in vitro techniques, such as Triton X-114 fractionation or tryptic shaving followed by immunoblotting. Our in vitro results unambiguously support the finding that GlpO is a cytoplasmic protein throughout the “ Mycoplasma mycoides cluster.” Thus, the use of GlpO as a candidate vaccine antigen is unlikely to induce a protective immune response.

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“…Biological characteristics of certain nucleases in mycoplasmas.Certain mycoplasma can also express various antioxidant enzymes including methionine sulfoxide reductase (MsrA), organic hydroperoxide reductase (Ohr), osmotically inducible protein C (OsmC), superoxide dismutase (SOD), catalase, ClpB, thioredoxin reductase, thiol peroxidase, and peroxiredoxin[85,124,[143][144][145][146]. These enzymes can effectively protect mycoplasmas from oxidative damage imposed by the host, and significantly increase their survival in the host.…”

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Infection strategies of mycoplasmas: Unraveling the panoply of virulence factors

Chen

Qin

et al. 2021

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Mycoplasmas, the smallest bacteria lacking a cell wall, can cause various diseases in both humans and animals. Mycoplasmas harbor a variety of virulence factors that enable them to overcome numerous barriers of entry into the host; using accessory proteins, mycoplasma adhesins can bind to the receptors or extracellular matrix of the host cell. Although the host immune system can eradicate the invading mycoplasma in most cases, a few sagacious mycoplasmas employ a series of invasion and immune escape strategies to ensure their continued survival within their hosts. For instance, capsular polysaccharides are crucial for anti-phagocytosis and immunomodulation. Invasive enzymes degrade reactive oxygen species, neutrophil extracellular traps, and immunoglobulins. Biofilm formation is important for establishing a persistent infection. During proliferation, successfully surviving mycoplasmas generate numerous metabolites, including hydrogen peroxide, ammonia and hydrogen sulfide; or secrete various exotoxins, such as communityacquired respiratory distress syndrome toxin, and hemolysins; and express various pathogenic enzymes, all of which have potent toxic effects on host cells. Furthermore, some inherent components of mycoplasmas, such as lipids, membrane lipoproteins, and even mycoplasmagenerated superantigens, can exert a significant pathogenic impact on the host cells or the immune system. In this review, we describe the proposed virulence factors in the toolkit of notorious mycoplasmas to better understand the pathogenic features of these bacteria, along with their pathogenic mechanisms.

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A peroxiredoxin from Mycoplasma hyopneumoniae with a possible role in H2O2 detoxification

Cited by 15 publications

References 39 publications

Comparative proteomic analysis of pathogenic and non-pathogenic strains from the swine pathogen Mycoplasma hyopneumoniae

Comparative proteomic analysis of pathogenic and non-pathogenic strains from the swine pathogen Mycoplasma hyopneumoniae

Evidence for the Cytoplasmic Localization of the L-α-Glycerophosphate Oxidase in Members of the “Mycoplasma mycoides Cluster”

Infection strategies of mycoplasmas: Unraveling the panoply of virulence factors

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