PapG adhesin from E. coli J96 recognizes the same saccharide epitope when present on whole bacteria and as isolated protein.
Purified PapG adhesin from the genetically well-defined uropathogenic Escherichia coli strain J96, as well as whole bacteria, were bound to microtiter plates that carried covalently bound globotetraose and galabiose. The binding was inhibited by soluble saccharide derivatives corresponding to the glycolipids, including all di-, tri-, tetra-, and pentasaccharide fragments of the Forssman antigen and all monodeoxy analogues of galabiose. Analysis of the inhibition pattern showed no significant difference between purified adhesin and whole bacteria. The glucose unit at the reducing end of the natural saccharides was detrimental to PapG binding since deletion of the glucose unit increased the inhibitory power 10-20 fold. The five hydroxyl groups HO-6, -2', -3', -4', -6' of the galabiose unit were shown to be important for PapG binding, presumably via intermolecular hydrogen bonds.
Nilsson
U
U
Center for Chemistry and Chemical Engineering, Lund University, Sweden.
Striker
R T
RT
Hultgren
S J
SJ
Magnusson
G
G
D018830:Adhesins, Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry*; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000737:chemistry / Q000378:metabolism*; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data
D018830:Adhesins, Escherichia coli; D000939:Epitopes; C092426:PapG protein, E coli; D036781:Fimbriae Proteins