Bacterial outer membrane protein (OMP)

Bacterial outer membrane proteins (OMPs) are essential integral proteins found in the outer membrane of Gram-negative bacteria, typically characterized by a beta-barrel structural motif [1]. They serve diverse and critical roles, including acting as porins for the passive diffusion of nutrients and hydrophilic drugs, functioning as active transporters for essential molecules like iron, and maintaining the structural integrity of the bacterial cell envelope [2, 3]. OMPs are also key virulence factors that facilitate bacterial attachment to host tissues and help the pathogen evade the host immune system [4]. As therapeutic targets, OMPs are highly valuable because they are surface-exposed and often essential for bacterial survival; for example, the BAM complex is required for the proper folding and insertion of all OMPs into the membrane [5]. Recent pharmacological advancements have led to the development of novel antibiotics like darobactin and zosurabalpin, which target OMP assembly and transport pathways to overcome multi-drug resistance in pathogens such as Acinetobacter baumannii and Pseudomonas aeruginosa [6, 7]. Furthermore, OMPs are frequently investigated as primary antigens for the development of broad-spectrum antibacterial vaccines [8].

Other names

Outer membrane proteinsOMPsPorinsBacterial surface proteinsOuter membrane porinsBeta-barrel outer membrane proteins

Inhibition of the beta-barrel assembly machinery (BAM) complex, disruption of the lipopolysaccharide (LPS) transport (Lpt) pathway, or utilization of porin channels for antibiotic entry into the periplasm.