title: Recognition of receptor lipopolysaccharides by spike G protein of bacteriophage phiX174.
abstract: The spike G protein of bacteriophage phiX174 was prepared as a hexa histidine-tagged G protein (HisG). In the enzyme-linked plate assay, HisG bound specifically to lipopolysaccharides (LPSs) of the phiX174-sensitive strains, and did not bind to LPSs of the phiX174-insensitive strains. The truncated G protein obtained after trypsin digestion of HisG had the similar affinity to the LPSs to HisG, indicating that eight amino acid residues from the N-terminus are not essential to the binding with the LPSs.
authors.affiliation: Department of Bioscience, Mie University, Tsu, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Kawaura
authors.forename: M
authors.initials: M
authors.lastname: Inagaki
authors.forename: S
authors.initials: S
authors.lastname: Karita
authors.forename: M
authors.initials: M
authors.lastname: Kato
authors.forename: S
authors.initials: S
authors.lastname: Nishikawa
authors.forename: N
authors.initials: N
authors.lastname: Kashimura
mesh_terms: D010584:Bacteriophage phi X 174 / Q000502:physiology*; D001665:Binding Sites; D004926:Escherichia coli / Q000276:immunology; D007700:Kinetics; D008050:Lipid A / Q000378:metabolism; D008070:Lipopolysaccharides / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012486:Salmonella typhimurium / Q000276:immunology; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D008050:Lipid A; D008070:Lipopolysaccharides; D011994:Recombinant Proteins; D014764:Viral Proteins