The spike G protein of bacteriophage phi X174 was prepared as a hexa histid
ine-tagged G protein (HisG). In the enzyme-linked plate assay, HisG bound s
pecifically to lipopolysaccharides (LPSs) of the phi X174-sensitive strains
, and did not bind to LPSs of the phi X174-insensitive strains. The truncat
ed G protein obtained after trypsin digestion of HisG had the similar affin
ity to the LPSs to HisG, indicating that eight amino acid residues from the
N-terminus are not essential to the binding with the LPSs.