A review on metallo-β-lactamases

Abstract

The emergence and dissemination of antimicrobial resistance are problems of great importance worldwide, particularly between nosocomial pathogens of clinical importance such as nonfermentative Gram-negative bacilli and members of the family Enterobacteriaceae. The main mechanism of resistance these pathogens is the production of β-lactamases, which are enzymes that hydrolyzing the ring β-lactam hindering the action of antimicrobial β-lactam. The β- lactamases were classified into four classes of according its primary structure and may also be classified in two groups based on their catalytic mechanism, that is, serine-β-lactamases (Classes A, C and D) e metallo-β-lactamases (Class B). The metallo-β-lactamases (MβL) using ions divalentes, commonly zinc, as co-factor for its catalytic activity and currently represent one the most important class of enzymes, due of their ability to hydrolyze all antimicrobial β-lactam, including carbapenens, which are used in the treatment of Gram-negative bacteria multidrug-resistant and to remain stable before the serine-β-lactamases. The detection of samples producing of MβL helps infection control practioners to prevent the dissemination of this mechanism of resistance in the nosocomial environment and to prevent it come to the community, and emphasize the rational use of antimicrobial currently available for clinical use, since there are few investments in the pharmaceutical industry in search of new antimicrobial agents.