Antibacterial activity of 4,5-dihydroxy-2-cyclopentan-1-one (DHCP) and cloning of a gene conferring DHCP resistance in Escherichia coli

J Mol Microbiol Biotechnol. 2001 Jul;3(3):461-5.

Abstract

In the present study we report that 4,5-dihydroxy-2-cyclopentan-1-one (DHCP), which is derived from heat-treatment of uronic acid or its derivatives, has antibacterial activity against Escherichia coli. The compound causes complete growth inhibition at 350 microM concentration. We have cloned a gene from E. coli, which confers DHCP resistance when present in multicopy. The putative protein encoded by this gene (dep- DHCP efflux protein) is a transmembrane efflux protein with a high homology to other antibiotic-efflux proteins including those for chloramphenicol, bicyclomycin and tetracycline. However, the Dep protein does not confer cross-resistance to any of the antibiotics tested.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Carrier Proteins / chemistry
  • Cloning, Molecular
  • Cyclopentanes / pharmacology*
  • Drug Resistance, Microbial / genetics*
  • Escherichia coli / drug effects*
  • Escherichia coli / genetics*
  • Escherichia coli / growth & development
  • Escherichia coli Proteins*
  • Genomic Library
  • Kinetics
  • Membrane Proteins / chemistry
  • Membrane Transport Proteins*
  • Molecular Sequence Data
  • Peptide Library
  • Protein Conformation
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Software

Substances

  • 4,5-dihydroxy-2-cyclopentan-1-one
  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Carrier Proteins
  • Cyclopentanes
  • Escherichia coli Proteins
  • Mdfa protein, E coli
  • Membrane Proteins
  • Membrane Transport Proteins
  • Peptide Library
  • dep-DHCP efflux protein, E coli