Salmonella Newport outer membrane porin (OMP)

Salmonella Newport outer membrane porins are a family of pore-forming proteins, including OmpC, OmpF, and the Salmonella-specific OmpD, situated in the outer membrane of the Gram-negative bacterium Salmonella enterica serovar Newport [1][2]. These proteins form water-filled trimeric channels that allow for the passive diffusion of small hydrophilic molecules, such as sugars, ions, and amino acids, which are essential for bacterial metabolism and growth [2][4]. In clinical settings, these porins are critical because they serve as the primary gateway for many classes of antibiotics, including beta-lactams and fluoroquinolones, to enter the bacterial cell [2]. Salmonella Newport is a significant human pathogen often associated with foodborne outbreaks and multidrug resistance (MDR) [3]. Resistance is frequently achieved through the downregulation or structural modification of these porins, which limits drug uptake and renders standard treatments ineffective [2][4]. Because of their accessibility on the bacterial surface and their role in antibiotic entry, these porins are key targets for the development of potentiators that can bypass or restore membrane permeability, as well as candidates for subunit vaccines [1][4]. Sources: [1] UniProt (P0A264); [2] PubMed (PMID: 12834103); [3] CDC (Salmonella Newport Reports); [4] Journal of Bacteriology (Salmonella porin studies).

Other names

OmpCOmpFOmpDPorin proteinOuter membrane proteinSalmonella enterica serovar Newport porin

Facilitation of passive diffusion of hydrophilic antibiotics across the outer membrane to reach periplasmic or cytoplasmic targets.