Metallo-β-lactamases (Ambler’s class B, Bush-Jacoby’s classification group 3) are zinc-dependent enzymes able to hydrolyze a wide variety of β-lactam antibiotics, including oxyimino cephalosporins and carbapenems, while they are not inhibited by conventional β-lactamase inhibitors (e. g. clavulanic acid, tazobactam). Although resident metallo-β-lactamases have been reported in various bacterial species of limited clinical relevance, acquired metallo-β-lactamases (such as IMP- and VIM-type enzymes) begun to emerge in clinically-relevant opportunistic pathogens in the 90’s. Nowadays, metallo-β-lactamase-producing clinical isolates have been identified virtually worldwide, while new enzymes are still appearing in the clinical setting (e. g. NDM-1), consolidating the relevance of metallo-β-lactamases as a serious public health issue and emphasizing the need for specific clinically-useful inhibitors. The current knowledge on the functional and structural properties of metallo-β-lactamases will be reviewed, with a particular focus on the clinically-relevant enzymes such as IMP-1, VIM-2 and NDM-1. The latest data on the structure-function relationships of these enzymes, and their potential in the identification of metallo-β-lactamase inhibitors, will also be discussed.

Docquier, J.D. (2011). Structure and function of metallo-β-lactamases. Meet-the-Experts session “Structure, Function and Genetics of Metallo-β-Lactamases”.. In 51st Interscience Conference on Antimicrobial Agents and Chemotherapy Abstract Book.

Structure and function of metallo-β-lactamases. Meet-the-Experts session “Structure, Function and Genetics of Metallo-β-Lactamases”.

DOCQUIER, JEAN DENIS
2011-01-01

Abstract

Metallo-β-lactamases (Ambler’s class B, Bush-Jacoby’s classification group 3) are zinc-dependent enzymes able to hydrolyze a wide variety of β-lactam antibiotics, including oxyimino cephalosporins and carbapenems, while they are not inhibited by conventional β-lactamase inhibitors (e. g. clavulanic acid, tazobactam). Although resident metallo-β-lactamases have been reported in various bacterial species of limited clinical relevance, acquired metallo-β-lactamases (such as IMP- and VIM-type enzymes) begun to emerge in clinically-relevant opportunistic pathogens in the 90’s. Nowadays, metallo-β-lactamase-producing clinical isolates have been identified virtually worldwide, while new enzymes are still appearing in the clinical setting (e. g. NDM-1), consolidating the relevance of metallo-β-lactamases as a serious public health issue and emphasizing the need for specific clinically-useful inhibitors. The current knowledge on the functional and structural properties of metallo-β-lactamases will be reviewed, with a particular focus on the clinically-relevant enzymes such as IMP-1, VIM-2 and NDM-1. The latest data on the structure-function relationships of these enzymes, and their potential in the identification of metallo-β-lactamase inhibitors, will also be discussed.
2011
Docquier, J.D. (2011). Structure and function of metallo-β-lactamases. Meet-the-Experts session “Structure, Function and Genetics of Metallo-β-Lactamases”.. In 51st Interscience Conference on Antimicrobial Agents and Chemotherapy Abstract Book.
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/975418