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. 1988 Jun;56(6):1475–1484. doi: 10.1128/iai.56.6.1475-1484.1988

Isolation and nucleotide sequence of the F17-A gene encoding the structural protein of the F17 fimbriae in bovine enterotoxigenic Escherichia coli.

P Lintermans 1, P Pohl 1, F Deboeck 1, A Bertels 1, C Schlicker 1, J Vandekerckhove 1, J Van Damme 1, M Van Montagu 1, H De Greve 1
PMCID: PMC259424  PMID: 2897333

Abstract

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.

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