title: Conformation of Escherichia coli outer membrane protein OmpA produced in Bacillus subtilis: influence of lipopolysaccharide.
abstract: The conformation of the outer membrane protein OmpA of Escherichia coli produced in Bacillus subtilis and solubilized in Sarkosyl was studied by measuring its ability to bind OmpA-specific phage K3 and to inhibit F-mediated conjugation. The partially purified protein was inactive in both of these assays. Refolding of the protein in the presence of lipopolysaccharide resulted in preparations with full phage-binding and conjugation-inhibiting capacity, indicating the formation of surface-exposed loops of OmpA of native conformation. The finding is of importance for the potential use of outer membrane proteins of Gram-negative bacteria as vaccines.
authors.affiliation: Department of Molecular Bacteriology, National Public Health Institute, Helsinki, Finland.
authors.forename: R
authors.initials: R
authors.lastname: Puohiniemi
authors.forename: A
authors.initials: A
authors.lastname: Muotiala
authors.forename: I M
authors.initials: IM
authors.lastname: Helander
authors.forename: M
authors.initials: M
authors.lastname: Sarvas
mesh_terms: D001412:Bacillus subtilis / Q000378:metabolism; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000494:pharmacology; D003227:Conjugation, Genetic / Q000187:drug effects; D004926:Escherichia coli / Q000737:chemistry*; D008070:Lipopolysaccharides; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000494:pharmacology; D014162:Transfection
chemical_list: D001425:Bacterial Outer Membrane Proteins; D008070:Lipopolysaccharides; D011994:Recombinant Proteins