Recognition of Receptor Lipopolysaccharides by Spike G Protein of Bacteriophage φX174

Abstract

The spike G protein of bacteriophage φX174 was prepared as a hexa histidine-tagged G protein (HisG). In the enzyme-linked plate assay, HisG bound specifically to lipopolysaccharides (LPSs) of the φX174-sensitive strains, and did not bind to LPSs of the φX174-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.

• spike G protein
• φX174
• lipopolysaccharide
• enzyme-linked assay
• phage receptor