Verona integron-encoded metallo-beta-lactamase (VIM) (VIM)

Verona integron-encoded metallo-beta-lactamases (VIM) are a critical family of Class B carbapenemases that mediate high-level resistance to nearly all beta-lactam antibiotics, including carbapenems, which are often considered drugs of last resort. These enzymes are characterized by their requirement for zinc ions at the active site to catalyze the hydrolysis of the beta-lactam ring, a mechanism distinct from the serine-based hydrolysis used by Class A, C, and D enzymes (PubMed: 11134056). VIM variants are predominantly identified in Gram-negative opportunistic pathogens such as Pseudomonas aeruginosa, Acinetobacter baumannii, and various Enterobacteriaceae, often localized on mobile genetic elements that facilitate horizontal gene transfer (PubMed: 28923873). The designation Other VIM variants encompasses the wide array of emerging sequence diversities within this family, such as VIM-4 through VIM-70, which continue to evolve under selective pressure. Therapeutically, VIM enzymes are not inhibited by traditional inhibitors like tazobactam or avibactam; however, next-generation cyclic boronate inhibitors like taniborbactam and xeruborbactam are currently in development to address this unmet medical need (PubMed: 31615871). Monitoring the prevalence of these variants is essential for hospital infection control and the guidance of empirical antimicrobial therapy.

Other names

VIM-type metallo-beta-lactamaseblaVIMClass B1 carbapenemaseMetallo-beta-lactamase VIM

Inhibition of metallo-beta-lactamase activity through active-site binding and interference with zinc-mediated catalysis.