Thin aggregative fimbriae from diarrheagenic Escherichia coli.
Journal: 1992/August - Journal of Bacteriology
ISSN: 0021-9193
PUBMED: 1624441
Abstract:
Four strains of diarrheagenic Escherichia coli originally isolated from distinct geographic regions were found to produce unusual thin aggregative fimbriae requiring depolymerization in formic acid prior to analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Immunoelectron microscopy of native fimbriae and Western blot (immunoblot) analysis of the corresponding 18-kDa fimbrins showed that these E. coli fimbriae were serologically cross-reactive with SEF 17 (Salmonella enteritidis fimbriae with a fimbrin molecular mass of 17 kDa). The E. coli and S. enteritidis fimbrins had similar total amino acid compositions and highly conserved N-terminal amino acid sequences. These results indicate that E. coli and S. enteritidis produce biochemically related, aggregative fimbriae which constitute a new type of intergenerically distributed fimbriae for which we propose the descriptive name GVVPQ fimbriae on the basis of the conserved N-terminal amino acid sequence.
Relations:
Content
Citations
(23)
References
(33)
Conditions
(1)
Drugs
(2)
Chemicals
(3)
Organisms
(3)
Processes
(2)
Affiliates
(2)
Similar articles
Articles by the same authors
Discussion board
J Bacteriol 174(13): 4490-4495

Thin aggregative fimbriae from diarrheagenic Escherichia coli.

Abstract

Four strains of diarrheagenic Escherichia coli originally isolated from distinct geographic regions were found to produce unusual thin aggregative fimbriae requiring depolymerization in formic acid prior to analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Immunoelectron microscopy of native fimbriae and Western blot (immunoblot) analysis of the corresponding 18-kDa fimbrins showed that these E. coli fimbriae were serologically cross-reactive with SEF 17 (Salmonella enteritidis fimbriae with a fimbrin molecular mass of 17 kDa). The E. coli and S. enteritidis fimbrins had similar total amino acid compositions and highly conserved N-terminal amino acid sequences. These results indicate that E. coli and S. enteritidis produce biochemically related, aggregative fimbriae which constitute a new type of intergenerically distributed fimbriae for which we propose the descriptive name GVVPQ fimbriae on the basis of the conserved N-terminal amino acid sequence.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (2.8M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Aleksić S, Aleksić V. Reindarstellung und physikalisch-chemische Analyse des Fimbrien-Antigens bei zwei verschiedenen Enterobacteriaceae: Salmonella enteritidis und Yersinia enterocolitica. Zentralbl Bakteriol Orig A. 1979 Apr;243(2-3):177–196. [PubMed] [Google Scholar]
  • Aubel D, Darfeuille-Michaud A, Joly B. New adhesive factor (antigen 8786) on a human enterotoxigenic Escherichia coli O117:H4 strain isolated in Africa. Infect Immun. 1991 Apr;59(4):1290–1299.[PMC free article] [PubMed] [Google Scholar]
  • Bhaduri S, Turner-Jones C, Lachica RV. Convenient agarose medium for simultaneous determination of the low-calcium response and Congo red binding by virulent strains of Yersinia enterocolitica. J Clin Microbiol. 1991 Oct;29(10):2341–2344.[PMC free article] [PubMed] [Google Scholar]
  • Bilge SS, Clausen CR, Lau W, Moseley SL. Molecular characterization of a fimbrial adhesin, F1845, mediating diffuse adherence of diarrhea-associated Escherichia coli to HEp-2 cells. J Bacteriol. 1989 Aug;171(8):4281–4289.[PMC free article] [PubMed] [Google Scholar]
  • Boyer HW, Roulland-Dussoix D. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J Mol Biol. 1969 May 14;41(3):459–472. [PubMed] [Google Scholar]
  • Collinson SK, Emödy L, Müller KH, Trust TJ, Kay WW. Purification and characterization of thin, aggregative fimbriae from Salmonella enteritidis. J Bacteriol. 1991 Aug;173(15):4773–4781.[PMC free article] [PubMed] [Google Scholar]
  • de Graaf FK, Roorda I. Production, purification, and characterization of the fimbrial adhesive antigen F41 isolated from calf enteropathogenic Escherichia coli strain B41M. Infect Immun. 1982 May;36(2):751–758.[PMC free article] [PubMed] [Google Scholar]
  • Duguid JP, Anderson ES, Campbell I. Fimbriae and adhesive properties in Salmonellae. J Pathol Bacteriol. 1966 Jul;92(1):107–138. [PubMed] [Google Scholar]
  • Elliott SJ, Nandapalan N, Chang BJ. Production of type 1 fimbriae by Escherichia coli HB101. Microb Pathog. 1991 Jun;10(6):481–486. [PubMed] [Google Scholar]
  • Finlay BB, Falkow S. Common themes in microbial pathogenicity. Microbiol Rev. 1989 Jun;53(2):210–230.[PMC free article] [PubMed] [Google Scholar]
  • Gaastra W, de Graaf FK. Host-specific fimbrial adhesins of noninvasive enterotoxigenic Escherichia coli strains. Microbiol Rev. 1982 Jun;46(2):129–161.[PMC free article] [PubMed] [Google Scholar]
  • Girón JA, Ho AS, Schoolnik GK. An inducible bundle-forming pilus of enteropathogenic Escherichia coli. Science. 1991 Nov 1;254(5032):710–713. [PubMed] [Google Scholar]
  • Hall RH, Maneval DR, Jr, Collins JH, Theibert JL, Levine MM. Purification and analysis of colonization factor antigen I, coli surface antigen 1, and coli surface antigen 3 fimbriae from enterotoxigenic Escherichia coli. J Bacteriol. 1989 Nov;171(11):6372–6374.[PMC free article] [PubMed] [Google Scholar]
  • Heuzenroeder MW, Elliot TR, Thomas CJ, Halter R, Manning PA. A new fimbrial type (PCFO9) on enterotoxigenic Escherichia coli 09:H- LT+ isolated from a case of infant diarrhea in central Australia. FEMS Microbiol Lett. 1990 Jan 1;54(1-3):55–60. [PubMed] [Google Scholar]
  • Hinson G, Knutton S, Lam-Po-Tang MK, McNeish AS, Williams PH. Adherence to human colonocytes of an Escherichia coli strain isolated from severe infantile enteritis: molecular and ultrastructural studies of a fibrillar adhesin. Infect Immun. 1987 Feb;55(2):393–402.[PMC free article] [PubMed] [Google Scholar]
  • Isberg RR. Discrimination between intracellular uptake and surface adhesion of bacterial pathogens. Science. 1991 May 17;252(5008):934–938. [PubMed] [Google Scholar]
  • Kay WW, Phipps BM, Ishiguro EE, Trust TJ. Porphyrin binding by the surface array virulence protein of Aeromonas salmonicida. J Bacteriol. 1985 Dec;164(3):1332–1336.[PMC free article] [PubMed] [Google Scholar]
  • Klemm P. Fimbrial adhesions of Escherichia coli. Rev Infect Dis. 1985 May-Jun;7(3):321–340. [PubMed] [Google Scholar]
  • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. [PubMed] [Google Scholar]
  • Levine MM. Escherichia coli that cause diarrhea: enterotoxigenic, enteropathogenic, enteroinvasive, enterohemorrhagic, and enteroadherent. J Infect Dis. 1987 Mar;155(3):377–389. [PubMed] [Google Scholar]
  • Ljungh A, Emödy L, Steinruck H, Sullivan P, West B, Zetterberg E, Wadström T. Fibronectin, vitronectin, and collagen binding to Escherichia coli of intestinal and extraintestinal origin. Zentralbl Bakteriol. 1990 Oct;274(1):126–134. [PubMed] [Google Scholar]
  • Müller KH, Collinson SK, Trust TJ, Kay WW. Type 1 fimbriae of Salmonella enteritidis. J Bacteriol. 1991 Aug;173(15):4765–4772.[PMC free article] [PubMed] [Google Scholar]
  • Olsén A, Jonsson A, Normark S. Fibronectin binding mediated by a novel class of surface organelles on Escherichia coli. Nature. 1989 Apr 20;338(6217):652–655. [PubMed] [Google Scholar]
  • Pearson WR, Lipman DJ. Improved tools for biological sequence comparison. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2444–2448.[PMC free article] [PubMed] [Google Scholar]
  • Rafiee P, Leffler H, Byrd JC, Cassels FJ, Boedeker EC, Kim YS. A sialoglycoprotein complex linked to the microvillus cytoskeleton acts as a receptor for pilus (AF/R1) mediated adhesion of enteropathogenic Escherichia coli (RDEC-1) in rabbit small intestine. J Cell Biol. 1991 Nov;115(4):1021–1029.[PMC free article] [PubMed] [Google Scholar]
  • Scotland SM, Smith HR, Said B, Willshaw GA, Cheasty T, Rowe B. Identification of enteropathogenic Escherichia coli isolated in Britain as enteroaggregative or as members of a subclass of attaching-and-effacing E. coli not hybridising with the EPEC adherence-factor probe. J Med Microbiol. 1991 Nov;35(5):278–283. [PubMed] [Google Scholar]
  • Stugard CE, Daskaleros PA, Payne SM. A 101-kilodalton heme-binding protein associated with congo red binding and virulence of Shigella flexneri and enteroinvasive Escherichia coli strains. Infect Immun. 1989 Nov;57(11):3534–3539.[PMC free article] [PubMed] [Google Scholar]
  • Tarkkanen AM, Allen BL, Westerlund B, Holthöfer H, Kuusela P, Risteli L, Clegg S, Korhonen TK. Type V collagen as the target for type-3 fimbriae, enterobacterial adherence organelles. Mol Microbiol. 1990 Aug;4(8):1353–1361. [PubMed] [Google Scholar]
  • Taylor RK, Miller VL, Furlong DB, Mekalanos JJ. Use of phoA gene fusions to identify a pilus colonization factor coordinately regulated with cholera toxin. Proc Natl Acad Sci U S A. 1987 May;84(9):2833–2837.[PMC free article] [PubMed] [Google Scholar]
  • Thorns CJ, Sojka MG, Chasey D. Detection of a novel fimbrial structure on the surface of Salmonella enteritidis by using a monoclonal antibody. J Clin Microbiol. 1990 Nov;28(11):2409–2414.[PMC free article] [PubMed] [Google Scholar]
  • Väisänen-Rhen V. Fimbria-like hemagglutinin of Escherichia coli O75 strains. Infect Immun. 1984 Nov;46(2):401–407.[PMC free article] [PubMed] [Google Scholar]
  • Vial PA, Robins-Browne R, Lior H, Prado V, Kaper JB, Nataro JP, Maneval D, Elsayed A, Levine MM. Characterization of enteroadherent-aggregative Escherichia coli, a putative agent of diarrheal disease. J Infect Dis. 1988 Jul;158(1):70–79. [PubMed] [Google Scholar]
  • Yakubu DE, Senior BW, Old DC. A novel fimbrial haemagglutinin produced by a strain of Salmonella of serotype Salinatis. FEMS Microbiol Lett. 1989 Jan 1;48(1):29–33. [PubMed] [Google Scholar]
Department of Biochemistry and Microbiology, University of Victoria, British Columbia.
Department of Biochemistry and Microbiology, University of Victoria, British Columbia.
Abstract
Four strains of diarrheagenic Escherichia coli originally isolated from distinct geographic regions were found to produce unusual thin aggregative fimbriae requiring depolymerization in formic acid prior to analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Immunoelectron microscopy of native fimbriae and Western blot (immunoblot) analysis of the corresponding 18-kDa fimbrins showed that these E. coli fimbriae were serologically cross-reactive with SEF 17 (Salmonella enteritidis fimbriae with a fimbrin molecular mass of 17 kDa). The E. coli and S. enteritidis fimbrins had similar total amino acid compositions and highly conserved N-terminal amino acid sequences. These results indicate that E. coli and S. enteritidis produce biochemically related, aggregative fimbriae which constitute a new type of intergenerically distributed fimbriae for which we propose the descriptive name GVVPQ fimbriae on the basis of the conserved N-terminal amino acid sequence.
Collaboration tool especially designed for Life Science professionals.Drag-and-drop any entity to your messages.