TY - JOUR
T1 - Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase
T2 - A new molecular class B β-lactamase showing a broad substrate profile
AU - Rossolini, Gian Maria
AU - Franceschini, N.
AU - Riccio, M. L.
AU - Mercuri, P. S.
AU - Perilli, M.
AU - Galleni, M.
AU - Frere, Jean Marie
AU - Amicosante, G.
PY - 1998/5/15
Y1 - 1998/5/15
N2 - 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).
AB - 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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M3 - Article
C2 - 9576862
AN - SCOPUS:0032524824
VL - 332
SP - 145
EP - 152
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 1
ER -