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Inhibition of Adhesion of Type 1 Fimbriated Escherichia coli to Highly Mannosylated Ligands
Author(s) -
Nagahori Noriko,
Lee Reiko T.,
Nishimura ShinIchiro,
Pagé Daniel,
Roy René,
Lee Yuan C.
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020902)3:9<836::aid-cbic836>3.0.co;2-2
Subject(s) - escherichia coli , mannose , chemistry , dendrimer , bacterial adhesin , hemagglutination , lectin , biochemistry , biology , antigen , genetics , gene
The inhibitory potencies of a number of mannosides, di‐ and trivalent mannosides, a set of mannose‐terminating dendrimers, and five types of mannose‐bearing neoglycoproteins were determined by using a binding assay that measures the binding of 125 I‐labeled, highly mannosylated neoglycoprotein to a type 1 fimbriated Escherichia coli (K12) strain in suspension. The IC 50 values (the concentration of inhibitor that causes 50 % reduction in the bound 125 I‐ligand to E. coli ) obtained by this method were much lower than the equivalent values obtained by hemagglutination or in assays that involve microplate immobilization. Two important factors that strongly influence the affinity to E. coli adhesin are: 1) the presence of an α‐oriented aglycon that has a long aliphatic chain or an aromatic group immediately next to the glycosyl oxygen, and 2) the presence of multiple mannosyl residues that can span a distance of 20 nm or longer on a relatively inflexible structure. The two best inhibitors, which are a highly mannosylated neoglycoprotein with the longest linking arm between a mannose and protein amino group and the largest mannosylated dendrimer (fourth generation), exhibited sub‐n M IC 50 values.