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Escherichia coli and Salmonella Typhimurium cell membrane

Molecular classification
Other
01

Overview

The cell membrane (more precisely, the **outer membrane**) of uropathogenic Escherichia coli and Salmonella Typhimurium is a defining feature of these Gram-negative pathogens. It is an asymmetric bilayer with an outer leaflet rich in lipopolysaccharide (LPS) and a periplasmic leaflet of phospholipids, containing numerous outer membrane proteins (Omps), porins (e.g., OmpC, OmpF, OmpA), transporters, structural polysaccharides, flagella, and fimbriae. This outer membrane acts as a permeability barrier, affords protection against antibiotics and host defenses, and plays a key role in virulence, nutrient uptake, and evasion of immune recognition. Its structural components, such as LPS, core oligosaccharides, and porins, are targets of some antibiotics and serve as key determinants of antigenicity and resistance[5][3][6][4][2]. **Note:** This entry refers to a whole cell structure, not to a singular, well-defined molecular target. For structured therapeutic targeting, subcomponents such as “lipopolysaccharide,” “OmpA,” “OmpC,” or “IroN siderophore receptor” should be considered as individual molecular targets[2][5].

Other names
Gram-negative bacterial outer membraneE. coli outer membraneSalmonella outer membraneUPEC outer membrane
02

Mechanism of action

Disruption of membrane integrity (e.g., polymyxins disrupt outer membrane LPS and phospholipids) Inhibition of cell wall synthesis (entry of beta-lactams via porins) Permeabilization to facilitate antibiotic entry

03

Biological functions

Barrier functionStructural integrityTransport of moleculesImmune evasionModulation of host-pathogen interaction
04

Disease associations

InfectionAntibiotic resistance
05

Safety considerations

Difficult selective targeting—homology to commensal bacteriaResistance development via changes in membrane proteins and lipopolysaccharide structureNephrotoxicity of membrane-active antibiotics (e.g., polymyxins)
06

Interacting drugs

Polymyxins (e.g., colistin, polymyxin B)

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