Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 14553915Journal NLM ID: 7705721Publisher: Blackwell Publishing
Correspondence: inagaki
bio.mie-u.ac.jp
Institutions: Department of Life Science, Faculty of Bioresources, Mie University, 1515 Kamihama, Tsu, 514-8507, Mie, Japan
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
LPS, core, bacteriophage, proteins, G-protein, phiX174, host recognition, spike protein
Structure type: oligomer
Location inside paper: p.222, fig. 1
Aglycon: (->6) lipid A
Compound class: core oligosaccharide with O-unit
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_130693,IEDB_133751,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140088,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_232584,IEDB_983931,SB_192,SB_7
Methods: DOC-PAGE, enzyme-linked plate assay
Biological activity: the binding of spike H and G proteins
Related record ID(s): 7141, 7206, 7207, 7208, 7210, 7211, 7212, 7251
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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