Verona integron-encoded metallo-β-lactamase 1 (VIM-1) (VIM-1)

Verona integron-encoded metallo-β-lactamase 1 (VIM-1) is a critical enzyme involved in bacterial resistance against nearly all beta-lactam antibiotics, including carbapenems, which are often used as last-resort treatments for serious infections. It belongs to the Class B metallo-beta-lactamases (MBLs), characterized by the presence of zinc ions in the active site that facilitate the nucleophilic attack and subsequent hydrolysis of the beta-lactam ring (UniProt: P0C0L8). First identified in Italy in 1999, the blaVIM-1 gene is typically carried on mobile genetic elements such as integrons and plasmids, enabling its rapid dissemination among diverse Gram-negative pathogens like Pseudomonas aeruginosa and Klebsiella pneumoniae (PubMed: 10543752). Because VIM-1 is not inhibited by commercially available serine-beta-lactamase inhibitors like tazobactam or avibactam, it poses a significant challenge to modern medicine. Current drug development efforts are focused on novel pan-lactamase inhibitors, such as taniborbactam and xeruborbactam, which aim to neutralize MBLs and restore the efficacy of co-administered antibiotics (PubMed: 31988109).

Other names

Verona integron-encoded metallo-beta-lactamase 1blaVIM-1Metallo-beta-lactamase VIM-1VIM-1 MBL

Inhibition of the enzyme's catalytic activity by binding to the active site or chelating essential zinc ions, thereby preventing the hydrolysis of beta-lactam antibiotics and restoring their efficacy.