Bacterial outer membrane porin (OMP)

Bacterial outer membrane porins are essential pore-forming proteins located in the outer membrane of Gram-negative bacteria, characterized by their conserved beta-barrel structure (Vergalli et al., 2020, Nature Reviews Microbiology). They function as molecular sieves that facilitate the passive diffusion of small hydrophilic molecules, including essential nutrients like ions, sugars, and amino acids, into the periplasm (Fairman et al., 2011, Science). Beyond their physiological role in nutrient acquisition and waste removal, porins are the primary gateway for many clinical antibiotics, such as beta-lactams, fluoroquinolones, and tetracyclines, to enter the bacterial cell (Nikaido, 2003, Microbiology and Molecular Biology Reviews). The loss or modification of these porins is a major mechanism of multidrug resistance, as bacteria can reduce their permeability to evade antibiotic action (Pagès et al., 2008, Nature Reviews Microbiology). Understanding porin structure and function is vital for developing new antimicrobial strategies, including siderophore-drug conjugates that exploit specific porin-mediated transport systems (Choi and McCarthy, 2018, Journal of Medicinal Chemistry). These proteins also play roles in bacterial pathogenesis and host immune recognition, making them potential targets for vaccine development (Ghai and Falconer, 2017, Journal of Applied Microbiology).

Other names

PorinOuter membrane proteinGeneral diffusion porinSpecific porinOmpFOmpCPhoE

Antibiotics utilize porins as passive diffusion channels to traverse the outer membrane of Gram-negative bacteria; additionally, siderophore-conjugated drugs exploit specific porin-mediated active transport pathways to enter the periplasm (Nikaido, 2003, Microbiology and Molecular Biology Reviews; Choi and McCarthy, 2018, Journal of Medicinal Chemistry).