ArticleJournal of bacteriology2008
Structural and functional characterization of an organic hydroperoxide resistance protein from Mycoplasma gallisepticum.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 46 citations in OpenAlex.
- A sweeping view of avian mycoplasmas biology drawn from comparative genomic analyses.BMC genomics · 2025Article
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- Innate immune response in bovine neutrophils stimulated with Mycoplasma bovis.Veterinary research · 2021Article
- TheJournal of bacteriology · 2019Article
- Subversion of the Immune Response by Human Pathogenic Mycoplasmas.Frontiers in microbiology · 2019Review
- MIB-MIP is a mycoplasma system that captures and cleaves immunoglobulin G.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Factors associated with seroconversion to the major piroplasm surface protein of the bovine haemoparasite Theileria orientalis.Parasites & vectors · 2016Article
- Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae.Open biology · 2016Article
- A ferritin-like protein with antioxidant activity in Ureaplasma urealyticum.BMC microbiology · 2015Article
- Ohr Protects Corynebacterium glutamicum against Organic Hydroperoxide Induced Oxidative Stress.PloS one · 2015Article
- Inactivation of the organic hydroperoxide stress resistance regulator OhrR enhances resistance to oxidative stress and isoniazid in Mycobacterium smegmatis.Journal of bacteriology · 2015Article
- Functional characterization of osmotically inducible protein C (MG_427) from Mycoplasma genitalium.Journal of bacteriology · 2014Article
- Survey of surface proteins from the pathogenic Mycoplasma hyopneumoniae strain 7448 using a biotin cell surface labeling approach.PloS one · 2014Article
- Protection from oxidative stress relies mainly on derepression of OxyR-dependent KatB and Dps in Shewanella oneidensis.Journal of bacteriology · 2014Article
- OsmC proteins of Mycobacterium tuberculosis and Mycobacterium smegmatis protect against organic hydroperoxide stress.Tuberculosis (Edinburgh, Scotland) · 2011Article
- Mycoplasma gallisepticum infection in the grey partridge Perdix perdix: outbreak description, histopathology, biochemistry and antioxidant parameters.BMC veterinary research · 2011Article
- Organic hydroperoxide resistance protein and ergothioneine compensate for loss of mycothiol in Mycobacterium smegmatis mutants.Journal of bacteriology · 2011Article
- Macrophage replication screen identifies a novel Francisella hydroperoxide resistance protein involved in virulence.PloS one · 2011Article
- Comparative genomic analyses of attenuated strains of Mycoplasma gallisepticum.Infection and immunity · 2010Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As obligate parasites, Mycoplasma species are continuously exposed to oxidative damage due to host-generated peroxides and reactive oxygen species (ROS). In addition, the production of endogenous oxidants is believed to be a primary virulence mechanism of several Mollicute species, indicating that oxidative stress resistance is crucial to survival of these bacteria in the host milieu. Despite the abundance of oxidants at the site of infection, enzymes responsible for the detoxification of ROS have never been characterized in mycoplasmas. Here we characterize a homolog of the ohr (organic hydroperoxide resistance) family from Mycoplasma gallisepticum (encoding MGA1142). Unlike previously characterized ohr genes, the mga1142 gene is not upregulated in response to oxidative stress but displays a novel pattern of expression. Both organic and inorganic peroxides can act as substrates for MGA1142, but they are degraded with various efficiencies. Furthermore, cumene hydroperoxide, an aromatic peroxide metabolized with high efficiency by other Ohr proteins, was shown to rapidly inactivate MGA1142, accounting for the sensitivity of M. gallisepticum cells to this compound. Comparative modeling of the MGA1142 quaternary structure revealed that the active site of this molecule has a relatively wide conformation. These data indicate that the natural substrate for MGA1142 differs from that for previously characterized Ohr proteins. Triton X-114 partitioning demonstrated that MGA1142 is located in both cytosol and membrane fractions, suggesting that in vivo this molecule plays a role in the detoxification of both endogenous and exogenous peroxides. A model describing how MGA1142 is likely to be oriented in the cell membrane is presented.
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