Recognition of Receptor Lipopolysaccharides by Spike G Protein of Bacteriophage φX174
Copyright policy )Recognition of Receptor Lipopolysaccharides by Spike G Protein of Bacteriophage φX174
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.
- Mie University Japan
Lipopolysaccharides, Salmonella typhimurium, φX174, phage receptor, Binding Sites, spike G protein, lipopolysaccharide, enzyme-linked assay, Recombinant Proteins, Kinetics, Viral Proteins, Lipid A, Escherichia coli, Bacteriophage phi X 174
Lipopolysaccharides, Salmonella typhimurium, φX174, phage receptor, Binding Sites, spike G protein, lipopolysaccharide, enzyme-linked assay, Recombinant Proteins, Kinetics, Viral Proteins, Lipid A, Escherichia coli, Bacteriophage phi X 174
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