Open AccessDifferent contributions of the outer and inner R‐core residues of lipopolysaccharide to the recognition by spike H and G proteins of bacteriophage φ X174
Author(s) -
Inagaki Minoru,
Kawaura Tomoko,
Wakashima Hirohito,
Kato Muneharu,
Nishikawa Shiro,
Kashimura Naoki
Publication year - 2003
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00601-3
Subject(s) - escherichia coli , lipopolysaccharide , bacteriophage , inner core , bacterial outer membrane , strain (injury) , chemistry , biochemistry , microbiology and biotechnology , biology , gene , anatomy , geophysics , geology , endocrinology
The binding of spike H and G proteins of bacteriophage φ X174 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.