Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: A new molecular class B β-lactamase showing a broad substrate profile

Gian Maria Rossolini, N. Franceschini, M. L. Riccio, P. S. Mercuri, M. Perilli, M. Galleni, Jean Marie Frere, G. Amicosante

Research output: Contribution to journalArticle

Abstract

The metallo-β-lactamase produced by Chryseobacterium (formerly Flavobacterium) meningosepticum, which is the flavobacterial species of greatest clinical relevance, was purified and characterized. The enzyme, named BlaB, contains a polypeptide with an apparent M(r) of 26,000, and has a pI of 8.5. It hydrolyses penicillins, cephalosporins (including cefoxitin), carbapenems and 6-β-iodopenicillanate, a mechanism-based inactivator of active-site serine β-lactamases. The enzyme was inhibited by EDTA, 1-10 phenanthroline and pyridine-2,6-dicarboxylic acid, with different inactivation parameters for each chelating agent. The C. meningosepticum blaB gene was cloned and sequenced. According to the G + C content and codon usage, the blaB gene appeared to be endogenous to the species. The BlaB enzyme showed significant sequence similarity to other class B β-lactamases, being overall more similar to members of subclass B1, which includes the metallo-enzymes of Bacillus cereus (Be-II) and Bacteroides fragilis (CcrA) and the IMP-I enzyme found in various microbial species, and more distantly related to the metallo-β-lactamase of Aeromonas spp. (CphA, CphA2 and ImiS) and of Stenotrophomonas maltophilia (L1).

Original languageEnglish
Pages (from-to)145-152
Number of pages8
JournalBiochemical Journal
Volume332
Issue number1
Publication statusPublished - May 15 1998

ASJC Scopus subject areas

  • Biochemistry

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    Rossolini, G. M., Franceschini, N., Riccio, M. L., Mercuri, P. S., Perilli, M., Galleni, M., Frere, J. M., & Amicosante, G. (1998). Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: A new molecular class B β-lactamase showing a broad substrate profile. Biochemical Journal, 332(1), 145-152.