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Salmonella enterica outer membrane proteins (OMPs) and porins are essential structural and functional components of the bacterial cell envelope that mediate the interaction between the pathogen and its environment (Nikaido, 2003). Porins, such as OmpC, OmpF, and OmpD, are pore-forming proteins that facilitate the passive diffusion of small hydrophilic molecules, including essential nutrients and various classes of antibiotics like beta-lactams and fluoroquinolones (UniProt Consortium, 2023). These proteins are crucial for maintaining the osmotic balance and structural integrity of the bacterium while also playing significant roles in virulence, such as adhesion to host tissues and evasion of the host immune response (Verma et al., 2009). In clinical medicine, OMPs are primary targets for antibiotic entry; however, the downregulation or mutation of these porins is a major mechanism by which Salmonella develops multi-drug resistance (Nikaido, 2003). Furthermore, due to their high immunogenicity and exposure on the bacterial surface, OMPs are extensively studied as potential antigens for the development of vaccines against salmonellosis and typhoid fever (Verma et al., 2009).
Hydrophilic antibiotics such as beta-lactams and fluoroquinolones utilize porin channels to traverse the outer membrane and reach their intracellular targets, whereas polymyxins directly bind to the lipopolysaccharide and protein components of the outer membrane to disrupt its physical integrity.
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