Infection and Immunity · 2019 · 75 citations · 53 references
Life SciencesMicrobiologyMolecular BiologyBacteriologyHost-pathogen InteractionsMicrobial PathogenesisBiological MembranesLipid-protein InteractionsMembrane DomainsMembrane Protein TopologyMembrane ProteinsProtein-lipid InteractionsBacterial Membrane Lipid CompositionLipopolysaccharide BiosynthesisOuter Membrane ProteinsOuter Membrane StructurePeriplasmic PhysiologyPeriplasmic SpaceTransmembrane DomainsTransmembrane Proteins
Salmonella enterica serovar Typhimurium ( S . Typhimurium) relies upon the inner membrane protein PbgA to enhance outer membrane (OM) integrity and promote virulence in mice. The PbgA transmembrane domain (residues 1 to 190) is essential for viability, while the periplasmic domain (residues 191 to 586) is dispensable. Residues within the basic region (residues 191 to 245) bind acidic phosphates on polar phospholipids, like for cardiolipins, and are necessary for salmonella OM integrity. S .
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