Molecular and biochemical characterization of a novel class A beta-lactamase (HER-1) from Escherichia hermannii

Antimicrob Agents Chemother. 2003 Aug;47(8):2669-73. doi: 10.1128/AAC.47.8.2669-2673.2003.

Abstract

Escherichia hermannii showed a low level of resistance to amoxicillin and ticarcillin, reversed by clavulanate, and a moderate susceptibility to piperacillin but was susceptible to all cephalosporins. A bla gene was cloned and encoded a typical class A beta-lactamase (HER-1, pI 7.5), which shares 45, 44, 41, and 40% amino acid identity with other beta-lactamases, AER-1 from Aeromonas hydrophila, MAL-1/Cko-1 from Citrobacter koseri, and TEM-1 and LEN-1, respectively. No ampR gene was detected. Only penicillins were efficiently hydrolyzed, and no hydrolysis was observed for cefuroxime and broad-spectrum cephalosporins. Sequencing of the bla gene in 12 other strains showed 98 to 100% identity with bla(HER-1).

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology
  • DNA, Bacterial / genetics
  • DNA, Recombinant / genetics
  • Escherichia / drug effects
  • Escherichia / enzymology*
  • Escherichia / genetics*
  • Isoelectric Focusing
  • Kinetics
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Plasmids / genetics
  • beta-Lactamases / genetics*
  • beta-Lactamases / metabolism

Substances

  • Anti-Bacterial Agents
  • DNA, Bacterial
  • DNA, Recombinant
  • beta-Lactamases

Associated data

  • GENBANK/AF311385
  • GENBANK/AF398334
  • GENBANK/AF398335
  • GENBANK/AJ536088
  • GENBANK/AJ536089
  • GENBANK/AJ536090
  • GENBANK/AJ536091
  • GENBANK/AJ536092