title: Investigating the Role of Helicobacter pylori PriA Protein.
abstract: BACKGROUND
  In bacteria, PriA protein, a conserved DEXH-type DNA helicase, plays a central role in replication restart at stalled replication forks. Its unique DNA binding property allows it to recognize and stabilize stalled forks and the structures derived from them. PriA plays a very critical role in replication fork stabilization and DNA repair in E. coli and N. gonorrhoeae. In our in vivo expression technology screen, priA gene was induced in vivo when Helicobacter pylori infects mouse stomach.
  
  
  METHODS
  We decided to elucidate the role of H. pylori PriA protein in survival in mouse stomach, survival in gastric epithelial cells and macrophage cells, DNA repair, acid stress, and oxidative stress.
  
  
  RESULTS
  The priA null mutant strain was unable to colonize mice stomach mucosa after long-term infections. Mouse colonization was observed after 1 week of infection, but the levels were much lower than the wild-type HpSS1 strain. PriA protein was found to be important for intracellular survival of epithelial cell-/macrophage cell-ingested H. pylori. Also, a priA null mutant was more sensitive to DNA-damaging agents and was much more sensitive to acid and oxidative stress as compared to the wild-type strain.
  
  
  CONCLUSIONS
  These data suggest that the PriA protein is needed for survival and persistence of H. pylori in mice stomach mucosa.
authors.affiliation: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
authors.forename: Aparna
authors.initials: A
authors.lastname: Singh
authors.affiliation: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
authors.forename: Dusan
authors.initials: D
authors.lastname: Blaskovic
authors.affiliation: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
authors.forename: Jungsoo
authors.initials: J
authors.lastname: Joo
authors.affiliation: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
authors.forename: Zhen
authors.initials: Z
authors.lastname: Yang
authors.affiliation: National Institute on Minority Health and Health Disparities, National Institutes of Health, Bethesda, MD, USA.
authors.forename: Sharon H
authors.initials: SH
authors.lastname: Jackson
authors.affiliation: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.|National Institute on Minority Health and Health Disparities, National Institutes of Health, Bethesda, MD, USA.
authors.forename: William G
authors.initials: WG
authors.lastname: Coleman
authors.affiliation: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
authors.forename: Ming
authors.initials: M
authors.lastname: Yan
mesh_terms: D000818:Animals; D004265:DNA Helicases / Q000235:genetics / Q000378:metabolism*; D004260:DNA Repair; D004847:Epithelial Cells / Q000382:microbiology; D016480:Helicobacter pylori / Q000201:enzymology* / Q000502:physiology; D008264:Macrophages / Q000382:microbiology; D008810:Mice, Inbred C57BL; D050296:Microbial Viability; D018384:Oxidative Stress; D013270:Stomach / Q000382:microbiology; D037521:Virulence Factors / Q000235:genetics / Q000378:metabolism*
chemical_list: D037521:Virulence Factors; D004265:DNA Helicases
keywords: DNA helicase; Helicobacter pylori; replication fork stabilization
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