title: Specific interaction of fused H protein of bacteriophage phiX174 with receptor lipopolysaccharides.
abstract: The DNA fragment encoding the spike H protein of bacteriophage phiX174 was amplified by polymerase chain reaction. The fragment was sub-cloned into pQE-30 to yield pQE-H. The histidine-tagged H protein (HisH) was obtained from the cell extract of Escherichia coli M15 (pREP4) harboring pQE-H and purified by nickel chelating and anion-exchange chromatographies. HisH was shown to bind dose-dependently to the lipopolysaccharides (LPSs) isolated from phiX174-sensitive strains, E. coli C or Salmonella typhimurium TV119 (Ra mutant). In sharp contrast, HisH did not bind to the LPSs from insensitive strains, E. coli F583 (Rd2 mutant) or E. coli O111:B4 (smooth strain). Since the same selectivity was observed in the plaque counting assay for in vitro inactivation of phiX174, the spike H protein was shown to recognize receptor LPS.
authors.affiliation: Department of Bioscience, Mie University, Tsu, Japan.
authors.forename: R
authors.initials: R
authors.lastname: Suzuki
authors.forename: M
authors.initials: M
authors.lastname: Inagaki
authors.forename: S
authors.initials: S
authors.lastname: Karita
authors.forename: T
authors.initials: T
authors.lastname: Kawaura
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
authors.forename: J
authors.initials: J
authors.lastname: Morita
mesh_terms: D010584:Bacteriophage phi X 174 / Q000378:metabolism*; D002213:Capsid / Q000235:genetics / Q000378:metabolism*; D008070:Lipopolysaccharides / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D008070:Lipopolysaccharides; D011993:Recombinant Fusion Proteins