Abstract
The DNA fragment encoding the spike H protein of bacteriophage φX174 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 φX174-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 (Rd 2 mutant) or E. coli O111:B4 (smooth strain). Since the same selectivity was observed in the plaque counting assay for in vitro inactivation of φX174, the spike H protein was shown to recognize receptor LPS.
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