Different contributions of the outer and inner R-core residues of lipopolysaccharide to the recognition by spike H and G proteins of bacteriophage phiX174.
The binding of spike H and G proteins of bacteriophage phiX174 with lipopolysaccharides (LPSs) were evaluated by a competitive enzyme-linked plate assay using the biotin-labeled LPS of Escherichia coli C, one of a host strain, and the non-labeled LPSs having different R-core polysaccharide lengths. H protein promptly decreased its affinity when some saccharide residues were truncated from the outer R-core. However, G protein showed significant affinity to the LPSs lacking all the residues of the outer R-core and some of the inner R-core. Thus, G protein rather than H protein well recognized the residues of the inner R-core of LPS.
Inagaki
Minoru
M
Department of Life Science, Faculty of Bioresources, Mie University, 1515 Kamihama, Tsu, Mie 514-8507, Japan. inagaki@bio.mie-u.ac.jp
Kawaura
Tomoko
T
Wakashima
Hirohito
H
Kato
Muneharu
M
Nishikawa
Shiro
S
Kashimura
Naoki
N
D010584:Bacteriophage phi X 174 / Q000235:genetics / Q000254:growth & development / Q000502:physiology*; D001667:Binding, Competitive; D001710:Biotin / Q000378:metabolism; D002240:Carbohydrate Sequence; D004926:Escherichia coli / Q000737:chemistry; D008070:Lipopolysaccharides / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D011991:Receptors, Virus / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D012486:Salmonella typhimurium / Q000737:chemistry; D015678:Viral Structural Proteins / Q000302:isolation & purification / Q000378:metabolism*
D008070:Lipopolysaccharides; D011991:Receptors, Virus; D015678:Viral Structural Proteins; D001710:Biotin