A link between the assembly of flagella and lipooligosaccharide of the Gram-negative bacterium Campylobacter jejuni

Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):5160-5. doi: 10.1073/pnas.0913451107. Epub 2010 Mar 1.

Abstract

Campylobacter jejuni is the leading cause of acute bacterial diarrhea worldwide and is implicated in development of Guillain-Barré syndrome. Two major surface features, the outer membrane lipooligosaccharide and flagella, are highly variable and are often targets for modification. Presumably, these modifications provide a competitive advantage to the bacterium. In this work, we identify a gene encoding a phosphoethanolamine (pEtN) transferase (Cj0256) that serves a dual role in modifying not only the lipooligosaccharide lipid anchor lipid A with pEtN, but also the flagellar rod protein FlgG. Generation of a mutant in C. jejuni 81-176 by interruption of cj0256 resulted in the absence of pEtN modifications on lipid A as well as FlgG. The cj0256 mutant showed a 20-fold increase in sensitivity to the cationic antimicrobial peptide, polymyxin B, as well as a decrease in motility. Transmission EM of the cj0256 mutant revealed a population (approximately 95%) lacking flagella, indicating that, without pEtN modification of FlgG, flagella production is hindered. Most intriguing, this research identifies a pEtN transferase showing preference for two periplasmic substrates linking membrane biogenesis and flagellar assembly. Cj0256 is a member of a large family of mostly uncharacterized proteins that may play a larger role in the decoration of bacterial surface structures.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / metabolism
  • Campylobacter jejuni / drug effects
  • Campylobacter jejuni / enzymology
  • Campylobacter jejuni / metabolism*
  • Drug Resistance, Bacterial / drug effects
  • Escherichia coli / drug effects
  • Escherichia coli / metabolism
  • Ethanolaminephosphotransferase / metabolism
  • Ethanolamines / metabolism
  • Flagella / drug effects
  • Flagella / metabolism*
  • Gene Deletion
  • Lipid A / chemistry
  • Lipid A / metabolism
  • Lipopolysaccharides / chemistry
  • Lipopolysaccharides / metabolism*
  • Models, Biological
  • Movement / drug effects
  • Spectrometry, Mass, Electrospray Ionization
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Ethanolamines
  • Lipid A
  • Lipopolysaccharides
  • lipid-linked oligosaccharides
  • phosphorylethanolamine
  • Ethanolaminephosphotransferase