Identification of cptA, a PmrA-regulated locus required for phosphoethanolamine modification of the Salmonella enterica serovar typhimurium lipopolysaccharide core

J Bacteriol. 2005 May;187(10):3391-9. doi: 10.1128/JB.187.10.3391-3399.2005.

Abstract

In response to the in vivo environment, the Salmonella enterica serovar Typhimurium lipopolysaccharide (LPS) is modified. These modifications are controlled in part by the two-component regulatory system PmrA-PmrB, with the addition of 4-aminoarabinose (Ara4N) to the lipid A and phosphoethanolamine (pEtN) to the lipid A and core. Here we demonstrate that the PmrA-regulated STM4118 (cptA) gene is necessary for the addition of pEtN to the LPS core. pmrC, a PmrA-regulated gene necessary for the addition of pEtN to lipid A, did not affect core pEtN addition. Although imparting a similar surface charge modification as Ara4N, which greatly affects polymyxin B resistance and murine virulence, neither pmrC nor cptA plays a dramatic role in antimicrobial peptide resistance in vitro or virulence in the mouse model. Therefore, factors other than surface charge/electrostatic interaction contribute to resistance to antimicrobial peptides such as polymyxin B.

Publication types

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

MeSH terms

  • Animals
  • Anti-Bacterial Agents / metabolism
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism*
  • Drug Resistance, Bacterial
  • Endopeptidases / genetics*
  • Endopeptidases / metabolism*
  • Ethanolaminephosphotransferase / metabolism
  • Ethanolamines / metabolism
  • Female
  • Lipopolysaccharides / metabolism
  • Mice
  • Mice, Inbred BALB C
  • Neisseria meningitidis / enzymology
  • Paratyphoid Fever / microbiology*
  • Polymyxin B / metabolism
  • Salmonella typhimurium / genetics*
  • Salmonella typhimurium / metabolism*
  • Salmonella typhimurium / pathogenicity
  • Virulence

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Ethanolamines
  • Lipopolysaccharides
  • phosphorylethanolamine
  • Ethanolaminephosphotransferase
  • CptA protein, bacteria
  • Endopeptidases
  • Polymyxin B