The Salmonella enterica serovar typhimurium divalent cation transport systems MntH and SitABCD are essential for virulence in an Nramp1G169 murine typhoid model

Infect Immun. 2004 Sep;72(9):5522-5. doi: 10.1128/IAI.72.9.5522-5525.2004.

Abstract

Nramp1 is a transporter that pumps divalent cations from the vacuoles of phagocytic cells and is associated with the innate resistance of mice to diverse intracellular pathogens. We demonstrate that sitA and mntH, genes encoding high-affinity metal ion uptake systems in Salmonella enterica serovar Typhimurium, are upregulated when Salmonella is internalized by Nramp1-expressing macrophages and play an essential role in systemic infection of congenic Nramp1-expressing mice.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Bacterial Proteins*
  • Biological Transport
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cation Transport Proteins / genetics
  • Cation Transport Proteins / metabolism*
  • Cell Line
  • Disease Models, Animal
  • Humans
  • Macrophages / microbiology
  • Mice
  • Mice, Congenic
  • Mice, Inbred C57BL
  • Salmonella typhimurium / metabolism
  • Salmonella typhimurium / pathogenicity*
  • Typhoid Fever / microbiology
  • Virulence

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Cation Transport Proteins
  • MntH protein, bacteria
  • SitA protein, Shigella flexneri
  • natural resistance-associated macrophage protein 1