title: Purification and characterization of the Dr hemagglutinins expressed by two uropathogenic Escherichia coli strains.
abstract: The fibrillar Dr hemagglutinins expressed by two uropathogenic Escherichia coli isolates were mechanically sheared from whole cells and subsequently purified by using anion-exchange high-pressure liquid chromatography. The isolated hemagglutinins were proteins with apparent subunit molecular masses of 14,500 daltons by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric points of 5.4 in denaturing isoelectric focusing gels. The two proteins were serologically related to each other but distinct from P fimbriae, as assessed by bacterial agglutination and immunoblotting. The amino acid compositions of the two hemagglutinins were highly similar both to each other and to other Dr hemagglutinins. N-terminal amino acid sequencing of the major hemagglutinin subunit proteins demonstrated homology with afimbrial E. coli adhesins.
authors.affiliation: Department of Biochemistry, University of Toronto, Ontario, Canada.
authors.forename: M L
authors.initials: ML
authors.lastname: Kist
authors.forename: I E
authors.initials: IE
authors.lastname: Salit
authors.forename: T
authors.initials: T
authors.lastname: Hofmann
mesh_terms: D018830:Adhesins, Escherichia coli; D000371:Agglutination; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001425:Bacterial Outer Membrane Proteins / Q000032:analysis; D001789:Blood Group Antigens / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000276:immunology* / Q000648:ultrastructure; D006388:Hemagglutinins / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D008969:Molecular Sequence Data
chemical_list: D018830:Adhesins, Escherichia coli; D000596:Amino Acids; D001425:Bacterial Outer Membrane Proteins; D001789:Blood Group Antigens; D006388:Hemagglutinins