Isolation and characterization of F12 adhesive fimbrial antigen from uropathogenic Escherichia coli strains.
The adhesive fimbrial antigen F12 from a strain of uropathogenic Escherichia coli has been isolated and characterized. The antigen was purified by ammonium sulfate precipitation and gel chromatography. The protein subunit of the F12 fimbria has a molecular weight of 18,200; the N-terminal amino acid sequence of the subunit shows close resemblance to that of the subunits of other F fimbriae and the type 1 fimbriae. We identified in these proteins a pattern of alternating conserved and variable amino acid residues which could indicate a special structural and functional feature.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000942:Antigens, Bacterial / Q000032:analysis / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000254:growth & development / Q000276:immunology / Q000472:pathogenicity; D004927:Escherichia coli Infections / Q000209:etiology / Q000276:immunology* / Q000382:microbiology; D036781:Fimbriae Proteins; D006801:Humans; D007123:Immunoelectrophoresis, Two-Dimensional; D008970:Molecular Weight; D014552:Urinary Tract Infections / Q000209:etiology / Q000276:immunology* / Q000382:microbiology; D014774:Virulence
D000596:Amino Acids; D000942:Antigens, Bacterial; C022924:colonization factor antigens; D036781:Fimbriae Proteins