Recognition of receptor lipopolysaccharides by spike G protein of bacteriophage phiX174

Biosci Biotechnol Biochem. 2000 Sep;64(9):1993-7. doi: 10.1271/bbb.64.1993.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteriophage phi X 174 / physiology*
  • Binding Sites
  • Escherichia coli / immunology
  • Kinetics
  • Lipid A / metabolism
  • Lipopolysaccharides / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Salmonella typhimurium / immunology
  • Viral Proteins / chemistry
  • Viral Proteins / genetics
  • Viral Proteins / metabolism*


  • Lipid A
  • Lipopolysaccharides
  • Recombinant Proteins
  • Viral Proteins