Identification of New Natural CphA Metallo-β-Lactamases CphA4 and CphA5 in Aeromonas veronii and Aeromonas hydrophila Isolates from Municipal Sewage in Central Italy

Antimicrob Agents Chemother. 2015 Aug;59(8):4990-3. doi: 10.1128/AAC.00628-15. Epub 2015 May 18.

Abstract

Two new natural CphA metallo-β-lactamases, the CphA4 and CphA5 enzymes, were identified in water samples from municipal sewage in central Italy. Compared to CphA, the CphA4 and CphA5 enzymes showed numerous point mutations. These enzymes have a narrow spectrum of substrates focused on carbapenems only. CphA5 showed kcat values about 40-, 12-, and 97-fold higher than those observed for CphA4 versus imipenem, ertapenem, and biapenem, respectively.

MeSH terms

  • Aeromonas hydrophila / drug effects
  • Aeromonas hydrophila / enzymology*
  • Aeromonas hydrophila / genetics
  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / genetics*
  • Carbapenems / pharmacology
  • Ertapenem
  • Imipenem / pharmacology
  • Italy
  • Molecular Sequence Data
  • Point Mutation / genetics
  • Sewage / microbiology*
  • Thienamycins / pharmacology
  • beta-Lactamases / genetics*
  • beta-Lactams / pharmacology

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Carbapenems
  • Sewage
  • Thienamycins
  • beta-Lactams
  • Imipenem
  • beta-Lactamases
  • cphA protein, Aeromonas hydrophila
  • Ertapenem
  • biapenem

Associated data

  • GENBANK/KM609958
  • GENBANK/KP771880
  • PDB/1X8G