Isolation and nucleotide sequence of the F17-A gene encoding the structural protein of the F17 fimbriae in bovine enterotoxigenic Escherichia coli.
The genetic determinant for production of the fimbrial F17 adhesive antigen was isolated from a bovine enterotoxigenic Escherichia coli strain. The F17-A gene, coding for the structural component of the F17 fimbrial adhesin, was cloned and sequenced. An open reading frame of 540 base pairs encoding a polypeptide of 180 amino acids, of which the NH2-terminal 21 residues are characteristic of a signal sequence, has been characterized. The mature protein lacks histidine, methionine, and tryptophan. A possible promoter and ribosome binding site as well as a possible site for termination of transcription are proposed. An important homology of the F17-A protein with fimA and papA fimbrial proteins was found. The N-terminal sequence of the mature F17-A pilin is extremely similar to the N-terminal sequence of the G fimbriae identified on human pyelonephritogenic E. coli strains.
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins; D001483:Base Sequence; D002417:Cattle; D002872:Chromosome Deletion; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000302:isolation & purification; D004767:Enterotoxemia / Q000235:genetics / Q000382:microbiology / Q000473:pathology; D004926:Escherichia coli / Q000235:genetics* / Q000472:pathogenicity / Q000648:ultrastructure; D010861:Fimbriae, Bacterial / Q000502:physiology* / Q000648:ultrastructure; D005796:Genes; D005798:Genes, Bacterial; D008969:Molecular Sequence Data
D001426:Bacterial Proteins; D004269:DNA, Bacterial