Molecular characterization of a carbapenem-hydrolyzing beta-lactamase from Chryseobacterium (Flavobacterium) indologenes

FEMS Microbiol Lett. 1999 Feb 15;171(2):127-32. doi: 10.1111/j.1574-6968.1999.tb13422.x.

Abstract

Chryseobacterium (Flavobacterium) indologenes 001 clinical strain was resistant to several beta-lactam classes including carbapenems. Shotgun cloning experiments of Sau3AI restricted genomic DNA of C. indologenes 001 into pBKCMV cloning vector followed by transformation into Escherichia coli DH10B gave one recombinant plasmid possessing a 4.2-kb DNA insert. It encoded a pI 7.2 beta-lactamase of 239 amino acids (IND-1) which is a metallo-enzyme with a broad spectrum beta-lactam hydrolysis profile. This class B carbapenem-hydrolyzing beta-lactamase shares the highest identity (43%) with BlaB from C. meningosepticum, thus showing heterogeneity of carbapenem-hydrolyzing beta-lactamases in Chryseobacterium spp.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Carbapenems / metabolism
  • Carbapenems / pharmacology*
  • Cloning, Molecular
  • Flavobacterium / drug effects
  • Flavobacterium / enzymology
  • Flavobacterium / genetics*
  • Gene Expression Regulation, Bacterial / drug effects
  • Genes, Bacterial / drug effects
  • Kinetics
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Plasmids
  • Recombinant Proteins
  • Restriction Mapping
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Transformation, Genetic
  • beta-Lactam Resistance / genetics*
  • beta-Lactamases / genetics*
  • beta-Lactamases / metabolism*

Substances

  • Carbapenems
  • Recombinant Proteins
  • beta-Lactamases

Associated data

  • GENBANK/AF099139