Conservation of a novel protein associated with an antibiotic efflux operon in Burkholderia cenocepacia

FEMS Microbiol Lett. 2005 Apr 15;245(2):337-44. doi: 10.1016/j.femsle.2005.03.027.

Abstract

Burkholderia cenocepacia is a significant problem in individuals with cystic fibrosis and is a member of the B. cepacia complex of closely related antibiotic resistant bacteria. A salicylate-regulated antibiotic efflux operon has been identified in B. cenocepacia and one of its four genes, llpE, is without parallel in previously reported efflux operons. PCR amplification and sequencing of llpE from B. cepacia complex isolates demonstrated the highest prevalence in B. cenocepacia with a high degree of sequence conservation. While at least one non-synonymous mutation was identified between isolates from different genomovars, only synonymous differences were identified within the IIIA and IIIB sub-groups of B. cenocepacia. Structural modeling suggests that LlpE is a member of the alpha/beta hydrolase enzyme family. Identification of strong structural homology to hydrolases and a high degree of conservation in B. cenocepacia suggests an enzymatic function for LlpE, benefiting survival in the cystic fibrosis lung.

Publication types

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

MeSH terms

  • Anti-Bacterial Agents / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Biological Transport, Active / genetics*
  • Burkholderia / chemistry
  • Burkholderia / genetics*
  • Burkholderia / metabolism
  • Conserved Sequence
  • DNA, Bacterial / chemistry
  • DNA, Bacterial / genetics
  • Genes, Bacterial
  • Humans
  • Hydrolases / chemistry
  • Hydrolases / genetics
  • Models, Molecular
  • Mutation
  • Operon*
  • Phylogeny
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • DNA, Bacterial
  • Hydrolases