Outer membrane protein (specifically encompassing families like OmpA, CarO, OprD, and others) of Acinetobacter baumannii (OMP (common for the general class); specific proteins include OmpA, CarO, OprD, Omp33-36, Omp38, AbuO, DcaP, OmpW)

Outer membrane proteins of Acinetobacter baumannii are a large, diverse family of beta-barrel porins and associated membrane molecules that play central roles in the bacterium's resistance to antibiotics, environmental stress, and interaction with host cells. Notable OMPs such as OmpA, CarO, and OprD mediate the diffusion of nutrients and antibiotics, modulate host immune responses, and contribute significantly to the virulence and resilience of A. baumannii in clinical settings. Mutational adaptation or differential expression of these OMPs is strongly linked to carbapenem and multidrug resistance, making them critical targets for therapeutic intervention but also presenting major challenges due to structural redundancy and functional overlap among family members[1][2][4][5]. For biomarker or drug development purposes, focus should be placed on individual OMPs (such as OmpA, Omp33, or CarO) with defined roles in pathogenesis and drug resistance.

Other names

Outer membrane proteins (OMPs)Porins (e.g., OmpA, CarO, OprD, Omp33, OmpW, etc.)Major OMPs may have individual names: OmpA, Omp33, CarO, AbuO, DcaP, OmpW, TolB, etc.

Reduced antibiotic influx (porin loss/mutation); coupling to efflux pumps to remove antibiotics from periplasm (OmpA and others); biofilm formation increases resistance; direct sequestration/siphoning of extracellular antibiotics via OMVs containing OMPs; change in membrane permeability affecting antibacterial entry.