Targeted mechanisms and novel therapeutic strategies against extended-spectrum beta-lactamases: From precise detection to intelligent management of bacterial resistance

Extended-spectrum beta-lactamases (ESBLs) are enzymes that resist beta-lactam antibiotics, including penicillins, cephalosporins, and carbapenems, and are produced by a variety of bacteria, including Escherichia coli and Klebsiella pneumoniae. Since ESBLs are often plasmid-borne, antibiotic resistance can spread across bacteria due to their ease of transfer. The intricate structure of ESBLs changes based on the type of bacterium that produces them. However, they all share a beta-lactamase core structure. ESBLs act by hydrolyzing the beta-lactam ring of antibiotics thereby rendering them ineffective. Detection of ESBL-producing bacteria is very important for effective treatment of infections. These enzymes can be identified through various diagnostic methods, such as phenotypic tests and molecular assays. The most common diagnostic method is an antimicrobial susceptibility test, which involves testing bacterial sensitivity to different antibiotics. Furthermore, the use of molecular testing techniques like polymerase chain reaction is growing in the identification of ESBLs. This paper provides a summary of ESBLs, including their structure, function, and diagnostic methods. Thus, it is critical to comprehend ESBLs in order to create therapies that effectively address illnesses brought on by bacteria that produce ESBL.