Identification and characterization of a new metallo-beta-lactamase, IND-5, from a clinical isolate of Chryseobacterium indologenes

Antimicrob Agents Chemother. 2007 Aug;51(8):2988-90. doi: 10.1128/AAC.00083-07. Epub 2007 Apr 30.

Abstract

A new natural IND-type metallo-beta-lactamase variant, IND-5, was identified in a clinical isolate of Chryseobacterium indologenes. IND-5 shared 92.8% and 92.4% amino acid homology with IND-1 and IND-3, respectively. Purified enzyme (pI = 8.8, M(r) = 25,000) was able to hydrolyze penicillins, some narrow- and expanded-spectrum cephalosporins, and carbapenems but not monobactams.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / metabolism
  • Anti-Bacterial Agents / pharmacology
  • Carbapenems / metabolism
  • Carbapenems / pharmacology
  • Cephalosporins / metabolism
  • Cephalosporins / pharmacology
  • Chryseobacterium / drug effects
  • Chryseobacterium / enzymology*
  • Chryseobacterium / isolation & purification*
  • Flavobacteriaceae Infections / microbiology*
  • Humans
  • Kinetics
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Penicillins / metabolism
  • Penicillins / pharmacology
  • Sequence Analysis, DNA
  • beta-Lactam Resistance
  • beta-Lactamases* / chemistry
  • beta-Lactamases* / genetics
  • beta-Lactamases* / isolation & purification
  • beta-Lactamases* / metabolism

Substances

  • Anti-Bacterial Agents
  • Carbapenems
  • Cephalosporins
  • Penicillins
  • beta-Lactamases

Associated data

  • GENBANK/AY504627