Molecular mechanisms of Campylobacter fetus surface layer protein expression

Mol Microbiol. 1997 Nov;26(3):433-40. doi: 10.1046/j.1365-2958.1997.6151958.x.

Abstract

Cells of the Gram-negative bacteria Campylobacter fetus are covered by monomolecular arrays of surface layer proteins (SLPs) critical for both persistence in their natural hosts and for virulence. For C. fetus cells, expression of SLPs essentially eliminates C3b binding and their antigenic variation thwarts host immunological defences. Each cell possesses multiple partially homologous and highly conserved SLP gene cassettes, tightly clustered in the genome, that encode SLPs of 97-149 kDa. These attach non-covalently via a conserved N-terminus to the cell wall lipopolysaccharide. Recent studies indicate that C. fetus reassorts a single promoter, controlling SLP expression, and one, or more, complete open reading frame strictly by DNA inversion, and that rearrangement is independent of the distance between sites of inversion. In contrast to previously reported programmed DNA inversion systems, inversion in C. fetus is recA-dependent. These rearrangements permit variation in protein expression from the family of SLP genes and suggest an expanding paradigm of programmed DNA rearrangements among microorganisms.

Publication types

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

MeSH terms

  • Animals
  • Antigenic Variation
  • Bacterial Outer Membrane Proteins / biosynthesis
  • Bacterial Outer Membrane Proteins / genetics*
  • Bacterial Outer Membrane Proteins / immunology
  • Bacterial Proteins*
  • Campylobacter fetus / genetics*
  • Campylobacter fetus / pathogenicity
  • Chromosome Inversion
  • Chromosomes, Bacterial
  • DNA, Bacterial
  • Gene Expression*
  • Gene Rearrangement
  • Membrane Glycoproteins*
  • Promoter Regions, Genetic
  • Recombination, Genetic
  • Virulence

Substances

  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • DNA, Bacterial
  • Membrane Glycoproteins
  • S-layer proteins