Beta-lactamase BlaMab (BlaMab) (BlaMab)

Beta-lactamase BlaMab (BlaMab) is a chromosomally encoded Class A enzyme produced by Mycobacterium abscessus, a rapidly growing non-tuberculous mycobacterium known for its extreme drug resistance (Soroka et al., 2014, Antimicrob Agents Chemother). This enzyme plays a critical role in the pathogen's defense by efficiently hydrolyzing a wide spectrum of beta-lactam antibiotics, including penicillins, cephalosporins, and carbapenems, rendering them ineffective (Dubée et al., 2015, J Antimicrob Chemother). BlaMab is characterized by its broad substrate profile and its relative insensitivity to traditional inhibitors like clavulanic acid and tazobactam. In clinical settings, particularly for patients with cystic fibrosis or chronic pulmonary disease, the presence of BlaMab necessitates the use of newer, more potent inhibitors such as avibactam or relebactam in combination with carbapenems (Lefebvre AL, et al., 2017, Antimicrob Agents Chemother). Targeting BlaMab is essential for restoring the efficacy of beta-lactam therapy against M. abscessus infections. Research continues to focus on the structural basis of its broad-spectrum activity to develop next-generation inhibitors (Papp-Wallace et al., 2018, ACS Infect Dis).

Other names

Bla_MabClass A beta-lactamase BlaMabMycobacterium abscessus beta-lactamase

Inhibition of beta-lactamase activity through covalent binding to the active-site serine residue, preventing the hydrolysis of co-administered beta-lactam antibiotics.