Recognition of receptor lipopolysaccharides by spike G protein of bacteriophage phiX174.
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.
Kawaura
T
T
Department of Bioscience, Mie University, Tsu, Japan.
Inagaki
M
M
Karita
S
S
Kato
M
M
Nishikawa
S
S
Kashimura
N
N
D010584:Bacteriophage phi X 174 / Q000502:physiology*; D001665:Binding Sites; D004926:Escherichia coli / Q000276:immunology; D007700:Kinetics; D008050:Lipid A / Q000378:metabolism; D008070:Lipopolysaccharides / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012486:Salmonella typhimurium / Q000276:immunology; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D008050:Lipid A; D008070:Lipopolysaccharides; D011994:Recombinant Proteins; D014764:Viral Proteins