Structural and functional study of the receptor binding site for FimH adhesin in uropathogenic strains of Escherichia coli.
We evaluated binding capacity of FimH-FocH hybrid adhesins during their interaction with model 1M and 3M substrates and epithelial cells. Introduction of the Glu89Lys point mutation into the fimH gene induced a new 1M-specific phenotype of adhesin. The role of a new pathoadaptive sign in the population of E. coli is discussed.
Trinchina
E V
EV
Russian University of People's Friendship; Washington State University, Seattle, USA.
D018830:Adhesins, Escherichia coli / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001422:Bacterial Adhesion / Q000502:physiology*; D001665:Binding Sites; D002478:Cells, Cultured; D004847:Epithelial Cells / Q000378:metabolism; D004926:Escherichia coli / Q000166:cytology / Q000235:genetics* / Q000378:metabolism* / Q000648:ultrastructure; D010861:Fimbriae, Bacterial / Q000235:genetics* / Q000378:metabolism; D005798:Genes, Bacterial; D014644:Genetic Variation; D008239:Lysine / Q000378:metabolism; D009061:Mouth Mucosa / Q000166:cytology; D009876:Operon; D017354:Point Mutation; D017434:Protein Structure, Tertiary; D011956:Receptors, Cell Surface / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D001743:Urinary Bladder / Q000166:cytology
D018830:Adhesins, Escherichia coli; D011956:Receptors, Cell Surface; D011994:Recombinant Proteins; D008239:Lysine