title: Alteration of the Helicobacter pylori membrane proteome in response to changes in environmental salt concentration.
abstract: OBJECTIVE
  Helicobacter pylori infection and a high dietary salt intake are each risk factors for the development of gastric cancer. We hypothesize that changes in environmental salt concentrations lead to alterations in the H. pylori membrane proteome.
  
  
  METHODS
  Label-free and iTRAQ methods were used to identify H. pylori proteins that change in abundance in response to alterations in environmental salt concentrations. In addition, we biotinylated intact bacteria that were grown under high- or low-salt conditions, and thereby analyzed salt-induced changes in the abundance of surface-exposed proteins.
  
  
  RESULTS
  Proteins with increased abundance in response to high salt conditions included CagA, the outer membrane protein HopQ, and fibronectin domain-containing protein HP0746. Proteins with increased abundance in response to low salt conditions included VacA, two VacA-like proteins (ImaA and FaaA), outer-membrane iron transporter FecA3, and several proteins involved in flagellar activity. Consistent with the proteomic data, bacteria grown in high salt conditions exhibited decreased motility compared to bacteria grown in lower salt conditions.
  
  
  CONCLUSIONS
  Alterations in the H. pylori membrane proteome in response to high salt conditions may contribute to the increased risk of gastric cancer associated with a high salt diet.
authors.affiliation: Department of Pathology, Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN, USA.
authors.forename: Bradley J
authors.initials: BJ
authors.lastname: Voss
authors.affiliation: Department of Medicine, Vanderbilt University School of Medicine, Nashville, TN, USA.
authors.forename: John T
authors.initials: JT
authors.lastname: Loh
authors.affiliation: Proteomics Laboratory, Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, USA.
authors.forename: Salisha
authors.initials: S
authors.lastname: Hill
authors.affiliation: Proteomics Laboratory, Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, USA.|Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.
authors.forename: Kristie L
authors.initials: KL
authors.lastname: Rose
authors.affiliation: Proteomics Laboratory, Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, USA.|Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.
authors.forename: W Hayes
authors.initials: WH
authors.lastname: McDonald
authors.affiliation: Department of Pathology, Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN, USA.|Department of Medicine, Vanderbilt University School of Medicine, Nashville, TN, USA.|Veterans Affairs Tennessee Valley Healthcare System, Nashville, TN, USA.
authors.forename: Timothy L
authors.initials: TL
authors.lastname: Cover
mesh_terms: D004305:Dose-Response Relationship, Drug; D016480:Helicobacter pylori / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism* / Q000502:physiology; D008565:Membrane Proteins / Q000378:metabolism*; D009068:Movement / Q000187:drug effects; D020543:Proteome / Q000378:metabolism*; D040901:Proteomics; D017673:Sodium Chloride, Dietary / Q000494:pharmacology*; D013045:Species Specificity
chemical_list: D008565:Membrane Proteins; D020543:Proteome; D017673:Sodium Chloride, Dietary
keywords: Gastric cancer; Mass spectrometry; Motility; Outer membrane proteins