Carbapenem-hydrolyzing class A beta-lactamase FRI-1 (FRI-1)

Carbapenem-hydrolyzing class A beta-lactamase FRI-1 is a serine beta-lactamase first identified in Enterobacter cloacae complex isolates in France (Dortet et al., 2012, Antimicrob. Agents Chemother.). It is characterized by its ability to hydrolyze a broad spectrum of beta-lactam antibiotics, including penicillins, cephalosporins, and carbapenems, which are critical for treating severe infections (Dortet et al., 2015, J. Antimicrob. Chemother.). The enzyme's activity is a significant driver of antimicrobial resistance, particularly in hospital settings where carbapenem-resistant Enterobacteriaceae (CRE) pose a major public health threat. FRI-1 is typically encoded on plasmids, which facilitates its rapid dissemination among different bacterial species via horizontal gene transfer. In clinical practice, FRI-1 is inhibited by modern beta-lactamase inhibitors such as avibactam and vaborbactam, which are often administered in combination with antibiotics like ceftazidime or meropenem to restore their efficacy (Pasteran et al., 2016, J. Clin. Microbiol.). Monitoring the prevalence of the blaFRI-1 gene is essential for infection control and guiding appropriate antibiotic therapy.

Other names

FRI-1 carbapenemaseFrench Friedberg-1 carbapenemaseblaFRI-1

Inhibition of the carbapenemase enzyme through binding to the active-site serine residue, thereby preventing the degradation of beta-lactam antibiotics and restoring their bactericidal activity.