IMP-1 metallo-beta-lactamase (IMP-1)

IMP-1 metallo-beta-lactamase is a zinc-dependent enzyme that confers broad-spectrum resistance to nearly all beta-lactam antibiotics, including carbapenems, which are vital for treating multi-drug resistant infections (Bush & Bradford, 2020). It belongs to the Ambler Class B beta-lactamases and was one of the first mobile metallo-beta-lactamases identified in Gram-negative bacteria like Pseudomonas aeruginosa and Klebsiella pneumoniae (UniProt Consortium, 2023). The enzyme's mechanism involves the coordination of zinc ions to facilitate the hydrolysis of the beta-lactam ring, effectively neutralizing the antibiotic before it can reach its target (Bahr et al., 2021). Because IMP-1 is often encoded on mobile genetic elements like integrons and plasmids, it spreads rapidly across different bacterial species, complicating infection control (Bush & Bradford, 2020). While traditional beta-lactamase inhibitors like clavulanic acid are ineffective against IMP-1, novel inhibitors such as taniborbactam and xeruborbactam are currently being evaluated in clinical trials to restore antibiotic efficacy (Hecker et al., 2020). Developing effective treatments against IMP-1-producing pathogens remains a high priority in the global effort to combat antimicrobial resistance.

Other names

Imipenemase-1Metallo-beta-lactamase IMP-1blaIMP-1Class B carbapenemase IMP-1IMP-1 MBL

Inhibition of the metallo-beta-lactamase enzyme to prevent the hydrolysis of beta-lactam antibiotics, thereby restoring the efficacy of co-administered carbapenems or other beta-lactams.