Verona integron-encoded metallo-β-lactamase 2 (VIM-2) (VIM-2)

Verona integron-encoded metallo-beta-lactamase 2 (VIM-2) is a critical enzyme belonging to the Class B metallo-beta-lactamases (MBLs), primarily found in Gram-negative pathogens such as Pseudomonas aeruginosa (UniProt P0C012). It utilizes zinc ions in its active site to catalyze the hydrolysis of almost all beta-lactam antibiotics, including carbapenems, which are vital for treating multidrug-resistant infections (PubMed: 21859858). VIM-2 is frequently encoded on mobile genetic elements, specifically integrons, which facilitates its dissemination across different bacterial species and contributes to the global crisis of antimicrobial resistance (PubMed: 10681326). Because VIM-2 renders most standard-of-care antibiotics ineffective, it is a high-priority target for the development of novel beta-lactamase inhibitors like taniborbactam and xeruborbactam (PubMed: 31615871). Therapeutic approaches involve combining these inhibitors with existing antibiotics to protect the drug from degradation and restore its bactericidal activity. However, the development of such inhibitors is complicated by the need for high selectivity to avoid interfering with essential human zinc-containing enzymes (PubMed: 27513466).

Other names

Metallo-beta-lactamase VIM-2blaVIM-2Verona integron-encoded metallo-beta-lactamase 2

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 (PubMed: 31615871).