title: Mycoplasma iowae: relationships among oxygen, virulence, and protection from oxidative stress.
abstract: The poultry-associated bacterium Mycoplasma iowae colonizes multiple sites in embryos, with disease or death resulting. Although M. iowae accumulates in the intestinal tract, it does not cause disease at that site, but rather only in tissues that are exposed to atmospheric O2. The activity of M. iowae catalase, encoded by katE, is capable of rapid removal of damaging H2O2 from solution, and katE confers a substantial reduction in the amount of H2O2 produced by Mycoplasma gallisepticum katE transformants in the presence of glycerol. As catalase-producing bacteria are often beneficial to hosts with inflammatory bowel disease, we explored whether M. iowae was exclusively protective against H2O2-producing bacteria in a Caenorhabditis elegans model, whether its protectiveness changed in response to O2 levels, and whether expression of genes involved in H2O2 metabolism and virulence changed in response to O2 levels. We observed that M. iowae was in fact protective against H2O2-producing Streptococcus pneumoniae, but not HCN-producing Pseudomonas aeruginosa, and that M. iowae cells grown in 1% O2 promoted survival of C. elegans to a greater extent than M. iowae cells grown in atmospheric O2. Transcript levels of an M. iowae gene encoding a homolog of Mycoplasma pneumoniae CARDS toxin were 5-fold lower in cells grown in low O2. These data suggest that reduced O2, representing the intestinal environment, triggers M. iowae to reduce its virulence capabilities, effecting a change from a pathogenic mode to a potentially beneficial one.
authors.affiliation: Department of Microbiology, Miami University, Oxford, OH, 45056, USA. rpritchard@kwc.edu.|Present address: Division of Natural Sciences and Mathematics, Kentucky Wesleyan College, Owensboro, KY, 42301, USA. rpritchard@kwc.edu.
authors.forename: Rachel E
authors.initials: RE
authors.lastname: Pritchard
authors.affiliation: Department of Microbiology, Miami University, Oxford, OH, 45056, USA. balishmf@miamioh.edu.
authors.forename: Mitchell F
authors.initials: MF
authors.lastname: Balish
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D017173:Caenorhabditis elegans / Q000378:metabolism / Q000382:microbiology*; D002374:Catalase / Q000235:genetics* / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D006861:Hydrogen Peroxide / Q000494:pharmacology; D045793:Mycoplasma iowae / Q000201:enzymology / Q000235:genetics*; D018384:Oxidative Stress; D010100:Oxygen / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D014774:Virulence
chemical_list: D001426:Bacterial Proteins; D006861:Hydrogen Peroxide; D002374:Catalase; D010100:Oxygen