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. 1984 Aug;159(2):482–487. doi: 10.1128/jb.159.2.482-487.1984

K88ab gene of Escherichia coli encodes a fimbria-like protein distinct from the K88ab fimbrial adhesin.

F R Mooi, M van Buuren, G Koopman, B Roosendaal, F K de Graaf
PMCID: PMC215670  PMID: 6086572

Abstract

The K88ab adhesin operon of Escherichia coli encodes for a fimbrial protein (the K88ab adhesin) which is involved in colonization of the porcine intestine. We characterized a structural gene (gene A) which is part of the K88ab adhesin operon and codes for an as yet unidentified polypeptide (pA). A mutation in gene A resulted in accumulation of K88ab adhesin subunits inside the cell. The nucleotide sequence of gene A was determined, and the deduced amino acid sequence suggested that pA is synthesized as a precursor containing a typical N-terminal signal peptide. The molecular weight of pA was calculated to be ca. 17,600. Gene A is preceded by a sequence showing homology with the consensus promoter. Fimbrial subunits from a number of E. coli strains have significant homology at their N- and C-termini. pA also contained some of these conserved sequences and showed a number of other similarities with fimbrial subunits. Therefore, it seems likely that the K88ab adhesin operon codes for a fimbrial subunit (pA) distinct from the K88ab adhesin subunit.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson M. J., Whitehead J. S., Kim Y. S. Interaction of Escherichia coli K88 antigen with porcine intestinal brush border membranes. Infect Immun. 1980 Sep;29(3):897–901. doi: 10.1128/iai.29.3.897-901.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bolivar F., Rodriguez R. L., Greene P. J., Betlach M. C., Heyneker H. L., Boyer H. W., Crosa J. H., Falkow S. Construction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene. 1977;2(2):95–113. [PubMed] [Google Scholar]
  3. Båga M., Normark S., Hardy J., O'Hanley P., Lark D., Olsson O., Schoolnik G., Falkow S. Nucleotide sequence of the papA gene encoding the Pap pilus subunit of human uropathogenic Escherichia coli. J Bacteriol. 1984 Jan;157(1):330–333. doi: 10.1128/jb.157.1.330-333.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Casadaban M. J., Cohen S. N. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J Mol Biol. 1980 Apr;138(2):179–207. doi: 10.1016/0022-2836(80)90283-1. [DOI] [PubMed] [Google Scholar]
  5. Dougan G., Sherratt D. The transposon Tn1 as a probe for studying ColE1 structure and function. Mol Gen Genet. 1977 Mar 7;151(2):151–160. doi: 10.1007/BF00338689. [DOI] [PubMed] [Google Scholar]
  6. Gold L., Pribnow D., Schneider T., Shinedling S., Singer B. S., Stormo G. Translational initiation in prokaryotes. Annu Rev Microbiol. 1981;35:365–403. doi: 10.1146/annurev.mi.35.100181.002053. [DOI] [PubMed] [Google Scholar]
  7. Hawley D. K., McClure W. R. Compilation and analysis of Escherichia coli promoter DNA sequences. Nucleic Acids Res. 1983 Apr 25;11(8):2237–2255. doi: 10.1093/nar/11.8.2237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jones G. W., Rutter J. M. Role of the K88 antigen in the pathogenesis of neonatal diarrhea caused by Escherichia coli in piglets. Infect Immun. 1972 Dec;6(6):918–927. doi: 10.1128/iai.6.6.918-927.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kehoe M., Winther M., Dougan G. Expression of a cloned K88ac adhesion antigen determinant: identification of a new adhesion cistron and role of a vector-encoded promoter. J Bacteriol. 1983 Sep;155(3):1071–1077. doi: 10.1128/jb.155.3.1071-1077.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Klemm P. Primary structure of the CFA1 fimbrial protein from human enterotoxigenic Escherichia coli strains. Eur J Biochem. 1982 May 17;124(2):339–348. doi: 10.1111/j.1432-1033.1982.tb06597.x. [DOI] [PubMed] [Google Scholar]
  11. Mooi F. R., Harms N., Bakker D., de Graaf F. K. Organization and expression of genes involved in the production of the K88ab antigen. Infect Immun. 1981 Jun;32(3):1155–1163. doi: 10.1128/iai.32.3.1155-1163.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Mooi F. R., Wijfjes A., de Graaf F. K. Identification and characterization of precursors in the biosynthesis of the K88ab fimbria of Escherichia coli. J Bacteriol. 1983 Apr;154(1):41–49. doi: 10.1128/jb.154.1.41-49.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Mooi F. R., Wouters C., Wijfjes A., de Graaf F. K. Construction and characterization of mutants impaired in the biosynthesis of the K88ab antigen. J Bacteriol. 1982 May;150(2):512–521. doi: 10.1128/jb.150.2.512-521.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Mooi F. R., de Graaf F. K., van Embden J. D. Cloning, mapping and expression of the genetic determinant that encodes for the K88ab antigen. Nucleic Acids Res. 1979 Mar;6(3):849–865. doi: 10.1093/nar/6.3.849. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Morgan W. D., Bear D. G., von Hippel P. H. Rho-dependent termination of transcription. I. Identification and characterization of termination sites for transcription from the bacteriophage lambda PR promoter. J Biol Chem. 1983 Aug 10;258(15):9553–9564. [PubMed] [Google Scholar]
  16. Sanger F., Coulson A. R., Barrell B. G., Smith A. J., Roe B. A. Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol. 1980 Oct 25;143(2):161–178. doi: 10.1016/0022-2836(80)90196-5. [DOI] [PubMed] [Google Scholar]
  17. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Stirm S., Orskov F., Orskov I., Birch-Andersen A. Episome-carried surface antigen K88 of Escherichia coli. 3. Morphology. J Bacteriol. 1967 Feb;93(2):740–748. doi: 10.1128/jb.93.2.740-748.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Stüber D., Bujard H. Organization of transcriptional signals in plasmids pBR322 and pACYC184. Proc Natl Acad Sci U S A. 1981 Jan;78(1):167–171. doi: 10.1073/pnas.78.1.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Tinoco I., Jr, Borer P. N., Dengler B., Levin M. D., Uhlenbeck O. C., Crothers D. M., Bralla J. Improved estimation of secondary structure in ribonucleic acids. Nat New Biol. 1973 Nov 14;246(150):40–41. doi: 10.1038/newbio246040a0. [DOI] [PubMed] [Google Scholar]
  21. de Graaf F. K., Krenn B. E., Klaasen P. Organization and expression of genes involved in the biosynthesis of K99 fimbriae. Infect Immun. 1984 Feb;43(2):508–514. doi: 10.1128/iai.43.2.508-514.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem. 1983 Jun 1;133(1):17–21. doi: 10.1111/j.1432-1033.1983.tb07424.x. [DOI] [PubMed] [Google Scholar]

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