| Literature DB >> 14553915 |
Minoru Inagaki1, Tomoko Kawaura, Hirohito Wakashima, Muneharu Kato, Shiro Nishikawa, Naoki Kashimura.
Abstract
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.Entities:
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Year: 2003 PMID: 14553915 DOI: 10.1016/S0378-1097(03)00601-3
Source DB: PubMed Journal: FEMS Microbiol Lett ISSN: 0378-1097 Impact factor: 2.742