title: Yersinia pseudotuberculosis mntH functions in intracellular manganese accumulation, which is essential for virulence and survival in cells expressing functional Nramp1.
abstract: Manganese has an important yet undefined role in the virulence of many bacterial pathogens. In this study we confirm that a null mutation in Yersinia pseudotuberculosis mntH reduces intracellular manganese accumulation. An mntH mutant was susceptible to killing by reactive oxygen species when grown under manganese-limited conditions. The mntH mutant was defective in survival and growth in macrophages expressing functional Nramp1, but in macrophages deficient in Nramp the bacteria were able to survive and replicate. In Galleria mellonella, the mntH mutant was attenuated. Taken together, these data suggest a role for manganese in Y. pseudotuberculosis during macrophage intracellular survival, protecting the bacteria from the antimicrobial products released during the respiratory burst.
authors.affiliation: School of Biosciences, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter EX4 4QD, UK.
authors.forename: Olivia L
authors.initials: OL
authors.lastname: Champion
authors.affiliation: Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK.
authors.forename: Andrey
authors.initials: A
authors.lastname: Karlyshev
authors.affiliation: Defence Science and Technology Laboratory, Porton Down, Salisbury SP4 0JQ, UK.
authors.forename: Ian A M
authors.initials: IAM
authors.lastname: Cooper
authors.affiliation: Defence Science and Technology Laboratory, Porton Down, Salisbury SP4 0JQ, UK.
authors.forename: Donna C
authors.initials: DC
authors.lastname: Ford
authors.affiliation: Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK.
authors.forename: Brendan W
authors.initials: BW
authors.lastname: Wren
authors.affiliation: Defence Science and Technology Laboratory, Porton Down, Salisbury SP4 0JQ, UK.
authors.forename: Melanie
authors.initials: M
authors.lastname: Duffield
authors.affiliation: Defence Science and Technology Laboratory, Porton Down, Salisbury SP4 0JQ, UK.
authors.forename: Petra C F
authors.initials: PCF
authors.lastname: Oyston
authors.affiliation: School of Biosciences, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter EX4 4QD, UK.
authors.forename: Richard W
authors.initials: RW
authors.lastname: Titball
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D027682:Cation Transport Proteins / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D055786:Gene Knockout Techniques; D005816:Genetic Complementation Test; D007915:Lepidoptera / Q000382:microbiology; D008264:Macrophages / Q000382:microbiology*; D008345:Manganese / Q000378:metabolism*; D051379:Mice; D050296:Microbial Viability; D018384:Oxidative Stress; D017382:Reactive Oxygen Species / Q000633:toxicity; D016019:Survival Analysis; D014774:Virulence; D015011:Yersinia pseudotuberculosis / Q000187:drug effects / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D000099173:Natural Resistance-associated Macrophage Protein 1
chemical_list: D001426:Bacterial Proteins; D027682:Cation Transport Proteins; D008345:Manganese; D017382:Reactive Oxygen Species; D000099173:Natural Resistance-associated Macrophage Protein 1; C433793:MntH protein, bacteria