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).
Rossolini, G.M., Franceschini, N., Riccio, M.L., Mercuri, P.S., Perilli, M.G., Galleni, M., et al. (1998). Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile. BIOCHEMICAL JOURNAL, 332(1), 145-152 [10.1042/bj3320145].
Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile
ROSSOLINI, GIAN MARIA;
1998-01-01
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).
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https://hdl.handle.net/11365/17516
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