Acinetobacter baumannii outer membrane proteins (AbOMPs)

Acinetobacter baumannii outer membrane proteins (AbOMPs) are a group of highly conserved proteins located on the surface of this Gram-negative bacterium, serving as essential components for its survival, virulence, and antibiotic resistance (Mani et al., 2021). These proteins include structural porins like OmpA, which facilitates biofilm formation and host cell adhesion, as well as complex assembly machineries like the BAM (beta-barrel assembly machinery) and Lpt (lipopolysaccharide transport) complexes (Geisinger & Isberg, 2017). Because A. baumannii is a leading cause of multidrug-resistant (MDR) nosocomial infections, these conserved OMPs have become primary targets for next-generation therapeutics. For example, the novel antibiotic zosurabalpin (RG6006) specifically targets the LptD/E complex to block the transport of lipopolysaccharides to the outer membrane, leading to bacterial cell death (Pahil et al., 2024). Similarly, the peptide darobactin targets BamA to disrupt the folding of essential outer membrane proteins (Imai et al., 2019). Other conserved OMPs, such as the iron-regulated transporter BauA, are exploited by "Trojan horse" antibiotics like cefiderocol to gain entry into the cell (Mani et al., 2021). These targets are particularly attractive because they are often essential for bacterial viability and are highly conserved across diverse clinical isolates, minimizing the immediate risk of target-based resistance (Singh et al., 2020).

Other names

Acinetobacter baumannii outer membrane proteinsAbOMPsConserved surface proteins of AcinetobacterOuter membrane protein A (OmpA)BamALptDBauA

Inhibition of the lipopolysaccharide (LPS) transport machinery via the LptD/E complex, disruption of outer membrane protein folding through the BamA subunit of the BAM complex, and exploitation of siderophore-mediated iron transporters like BauA for antibiotic delivery (Pahil et al., 2024; Imai et al., 2019; Mani et al., 2021).