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

Verona integron-encoded metallo-beta-lactamase 2 (VIM-2) is a zinc-dependent enzyme of the beta-lactamase superfamily, primarily found in Gram-negative pathogens such as _Pseudomonas aeruginosa_ and Enterobacteriaceae. It hydrolyzes and inactivates a broad spectrum of beta-lactam antibiotics, including carbapenems, cephalosporins, and penicillins, but not monobactams. VIM-2 is a monomeric enzyme containing two zinc-binding sites involved in catalysis, belonging to the B1 subclass of metallo-beta-lactamases. It is a significant driver of multidrug resistance in hospital-associated infections, and its activity is not inhibited by available clinical beta-lactamase inhibitors. Experimental inhibitors are in development, but as of 2024, there are no approved drugs that effectively block VIM-2. Detection of the VIM-2 gene or enzyme activity in bacteria serves as a key marker for multidrug-resistant infections. The spread of VIM-2 poses a severe public health challenge due to poor therapeutic options and high associated mortality.

Other names

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

Beta-lactam hydrolysis via zinc-activated water molecule: The zinc ion(s) in the active site activate water, which then hydrolyzes the beta-lactam ring of antibiotics, thereby inactivating the drug. Inhibitors: Experimental inhibitors bind and bridge the dinuclear zinc cluster, blocking catalysis.