Beta-lactamase OXA-58 (OXA-58) (OXA-58)

OXA-58 is a plasmid-encoded Ambler class D beta-lactamase, also known as an oxacillinase, primarily identified in Acinetobacter baumannii [1, 2]. It plays a critical role in conferring resistance to carbapenems, which are often considered last-resort antibiotics for treating severe infections [3, 4]. The enzyme functions by hydrolyzing the beta-lactam ring of various antibiotics, including penicillins and carbapenems like imipenem and meropenem, thereby inactivating them [2, 5]. OXA-58 is typically located in the periplasm but can also be released into the extracellular environment via outer membrane vesicles [7, 8]. This extracellular release can protect neighboring susceptible bacteria from antibiotic treatment, a phenomenon known as sheltering [7, 8]. Due to its association with multidrug-resistant hospital outbreaks and its ability to spread through horizontal gene transfer, OXA-58 is a significant target for the development of novel beta-lactamase inhibitors [6, 10]. Current therapeutic strategies often involve combinations of beta-lactams with newer inhibitors like durlobactam to overcome the resistance mediated by this enzyme [11, 12]. The presence of OXA-58 is a major driver of the carbapenem-resistant Acinetobacter baumannii (CRAB) phenotype, which is classified as a critical priority pathogen by the World Health Organization [1, 12].

Other names

Oxacillinase-58blaOXA-58Class D beta-lactamase OXA-58Carbapenem-hydrolyzing oxacillinase OXA-58CHDL

Hydrolysis of the beta-lactam ring of beta-lactam antibiotics, leading to antibiotic inactivation.