title: Latency of the lipid A deacylase PagL is involved in producing a robust permeation barrier in the outer membrane of Salmonella enterica.
abstract: Lipid A deacylase PagL, which detoxifies endotoxin, is latent in Salmonella enterica. This study determined the biological significance of this latency. PagL latency was beneficial for bacteria in producing a robust permeation barrier through lipid A modifications under host-mimetic conditions that induced the modification enzymes, including PagL.
authors.affiliation: Faculty of Pharmaceutical Sciences, Doshisha Women's College, Kyotanabe 610-0395, Japan. kkawasak@dwc.doshisha.ac.jp
authors.forename: Kiyoshi
authors.initials: K
authors.lastname: Kawasaki
authors.forename: Takayuki
authors.initials: T
authors.lastname: Manabe
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001425:Bacterial Outer Membrane Proteins / Q000502:physiology*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002265:Carboxylic Ester Hydrolases / Q000235:genetics / Q000378:metabolism*; D024901:Drug Resistance, Multiple, Bacterial; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology; D008055:Lipids / Q000737:chemistry; D008826:Microbial Sensitivity Tests; D015394:Molecular Structure; D010539:Permeability; D012486:Salmonella typhimurium / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*
chemical_list: D000900:Anti-Bacterial Agents; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D008055:Lipids; D002265:Carboxylic Ester Hydrolases; C424702:PagL protein, Salmonella typhimurium