Skip to main content
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1993 Dec 1;178(6):2115–2121. doi: 10.1084/jem.178.6.2115

Short consensus repeat-3 domain of recombinant decay-accelerating factor is recognized by Escherichia coli recombinant Dr adhesin in a model of a cell-cell interaction

PMCID: PMC2191283  PMID: 7504058

Abstract

A bacterial pathogen that is important in both urinary tract and intestinal infections is Escherichia coli which expresses Dr or related adhesins. In this report, we present a model for testing cell-cell interaction, using both molecularly characterized laboratory cells that express recombinant molecules of human decay-accelerating factor (DAF), and recombinant bacterial Dr colonization factors. Dr adhesin ligand was identified as DAF (CD55), a membrane protein that protects autologous tissues from damage due to the complement system. Structure- function studies mapped the adhesin-binding site on the DAF molecule. A single-point substitution in the third short consensus repeat domain, Ser165 to Leu, corresponding to the Dra to Drb allelic polymorphism, caused complete abolition of adhesin binding to DAF.

Full Text

The Full Text of this article is available as a PDF (1,015.0 KB).

Selected References

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

  1. Aronson M., Medalia O., Schori L., Mirelman D., Sharon N., Ofek I. Prevention of colonization of the urinary tract of mice with Escherichia coli by blocking of bacterial adherence with methyl alpha-D-mannopyranoside. J Infect Dis. 1979 Mar;139(3):329–332. doi: 10.1093/infdis/139.3.329. [DOI] [PubMed] [Google Scholar]
  2. Bilge S. S., Clausen C. R., Lau W., Moseley S. L. 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. doi: 10.1128/jb.171.8.4281-4289.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Clausen C. R., Christie D. L. Chronic diarrhea in infants caused by adherent enteropathogenic Escherichia coli. J Pediatr. 1982 Mar;100(3):358–361. doi: 10.1016/s0022-3476(82)80429-0. [DOI] [PubMed] [Google Scholar]
  4. Coyne K. E., Hall S. E., Thompson S., Arce M. A., Kinoshita T., Fujita T., Anstee D. J., Rosse W., Lublin D. M. Mapping of epitopes, glycosylation sites, and complement regulatory domains in human decay accelerating factor. J Immunol. 1992 Nov 1;149(9):2906–2913. [PubMed] [Google Scholar]
  5. Daniels G. L., Tohyama H., Uchikawa M. A possible null phenotype in the Cromer blood group complex. Transfusion. 1982 Sep-Oct;22(5):362–363. doi: 10.1046/j.1537-2995.1982.22583017458.x. [DOI] [PubMed] [Google Scholar]
  6. Felgner P. L., Gadek T. R., Holm M., Roman R., Chan H. W., Wenz M., Northrop J. P., Ringold G. M., Danielsen M. Lipofection: a highly efficient, lipid-mediated DNA-transfection procedure. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7413–7417. doi: 10.1073/pnas.84.21.7413. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hoffman E. M. Inhibition of complement by a substance isolated from human erythrocytes. I. Extraction from human erythrocyte stromata. Immunochemistry. 1969 May;6(3):391–403. doi: 10.1016/0019-2791(69)90296-1. [DOI] [PubMed] [Google Scholar]
  8. Horstmann R. D., Sievertsen H. J., Knobloch J., Fischetti V. A. Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1657–1661. doi: 10.1073/pnas.85.5.1657. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Karr J. F., Nowicki B. J., Truong L. D., Hull R. A., Moulds J. J., Hull S. I. pap-2-encoded fimbriae adhere to the P blood group-related glycosphingolipid stage-specific embryonic antigen 4 in the human kidney. Infect Immun. 1990 Dec;58(12):4055–4062. doi: 10.1128/iai.58.12.4055-4062.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kinoshita T., Medof M. E., Silber R., Nussenzweig V. Distribution of decay-accelerating factor in the peripheral blood of normal individuals and patients with paroxysmal nocturnal hemoglobinuria. J Exp Med. 1985 Jul 1;162(1):75–92. doi: 10.1084/jem.162.1.75. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Korhonen T. K., Nurmiaho E. L., Ranta H., Edén C. S. New Method for isolation of immunologically pure pili from Escherichia coli. Infect Immun. 1980 Feb;27(2):569–575. doi: 10.1128/iai.27.2.569-575.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Labigne-Roussel A., Schmidt M. A., Walz W., Falkow S. Genetic organization of the afimbrial adhesin operon and nucleotide sequence from a uropathogenic Escherichia coli gene encoding an afimbrial adhesin. J Bacteriol. 1985 Jun;162(3):1285–1292. doi: 10.1128/jb.162.3.1285-1292.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lublin D. M., Atkinson J. P. Decay-accelerating factor and membrane cofactor protein. Curr Top Microbiol Immunol. 1990;153:123–145. doi: 10.1007/978-3-642-74977-3_7. [DOI] [PubMed] [Google Scholar]
  14. Lublin D. M., Coyne K. E. Phospholipid-anchored and transmembrane versions of either decay-accelerating factor or membrane cofactor protein show equal efficiency in protection from complement-mediated cell damage. J Exp Med. 1991 Jul 1;174(1):35–44. doi: 10.1084/jem.174.1.35. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lublin D. M., Krsek-Staples J., Pangburn M. K., Atkinson J. P. Biosynthesis and glycosylation of the human complement regulatory protein decay-accelerating factor. J Immunol. 1986 Sep 1;137(5):1629–1635. [PubMed] [Google Scholar]
  16. Lublin D. M., Thompson E. S., Green A. M., Levene C., Telen M. J. Dr(a-) polymorphism of decay accelerating factor. Biochemical, functional, and molecular characterization and production of allele-specific transfectants. J Clin Invest. 1991 Jun;87(6):1945–1952. doi: 10.1172/JCI115220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Lund B., Marklund B. I., Strömberg N., Lindberg F., Karlsson K. A., Normark S. Uropathogenic Escherichia coli can express serologically identical pili of different receptor binding specificities. Mol Microbiol. 1988 Mar;2(2):255–263. doi: 10.1111/j.1365-2958.1988.tb00027.x. [DOI] [PubMed] [Google Scholar]
  18. Nicholson-Weller A., Burge J., Austen K. F. Purification from guinea pig erythrocyte stroma of a decay-accelerating factor for the classical c3 convertase, C4b,2a. J Immunol. 1981 Nov;127(5):2035–2039. [PubMed] [Google Scholar]
  19. Nicholson-Weller A., Burge J., Fearon D. T., Weller P. F., Austen K. F. Isolation of a human erythrocyte membrane glycoprotein with decay-accelerating activity for C3 convertases of the complement system. J Immunol. 1982 Jul;129(1):184–189. [PubMed] [Google Scholar]
  20. Nicholson-Weller A., March J. P., Rosenfeld S. I., Austen K. F. Affected erythrocytes of patients with paroxysmal nocturnal hemoglobinuria are deficient in the complement regulatory protein, decay accelerating factor. Proc Natl Acad Sci U S A. 1983 Aug;80(16):5066–5070. doi: 10.1073/pnas.80.16.5066. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Nowicki B., Barrish J. P., Korhonen T., Hull R. A., Hull S. I. Molecular cloning of the Escherichia coli O75X adhesin. Infect Immun. 1987 Dec;55(12):3168–3173. doi: 10.1128/iai.55.12.3168-3173.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Nowicki B., Hull R., Moulds J. Use of the Dr hemagglutinin of uropathogenic Escherichia coli to differentiate normal from abnormal red cells in paroxysmal nocturnal hemoglobinuria. N Engl J Med. 1988 Nov 10;319(19):1289–1290. doi: 10.1056/NEJM198811103191916. [DOI] [PubMed] [Google Scholar]
  23. Nowicki B., Labigne A., Moseley S., Hull R., Hull S., Moulds J. The Dr hemagglutinin, afimbrial adhesins AFA-I and AFA-III, and F1845 fimbriae of uropathogenic and diarrhea-associated Escherichia coli belong to a family of hemagglutinins with Dr receptor recognition. Infect Immun. 1990 Jan;58(1):279–281. doi: 10.1128/iai.58.1.279-281.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Nowicki B., Moulds J., Hull R., Hull S. A hemagglutinin of uropathogenic Escherichia coli recognizes the Dr blood group antigen. Infect Immun. 1988 May;56(5):1057–1060. doi: 10.1128/iai.56.5.1057-1060.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Pangburn M. K., Schreiber R. D., Müller-Eberhard H. J. Deficiency of an erythrocyte membrane protein with complement regulatory activity in paroxysmal nocturnal hemoglobinuria. Proc Natl Acad Sci U S A. 1983 Sep;80(17):5430–5434. doi: 10.1073/pnas.80.17.5430. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Pere A., Nowicki B., Saxén H., Siitonen A., Korhonen T. K. Expression of P, type-1, and type-1C fimbriae of Escherichia coli in the urine of patients with acute urinary tract infection. J Infect Dis. 1987 Oct;156(4):567–574. doi: 10.1093/infdis/156.4.567. [DOI] [PubMed] [Google Scholar]
  27. Spring F. A., Judson P. A., Daniels G. L., Parsons S. F., Mallinson G., Anstee D. J. A human cell-surface glycoprotein that carries Cromer-related blood group antigens on erythrocytes and is also expressed on leucocytes and platelets. Immunology. 1987 Oct;62(2):307–313. [PMC free article] [PubMed] [Google Scholar]
  28. Swanson T. N., Bilge S. S., Nowicki B., Moseley S. L. Molecular structure of the Dr adhesin: nucleotide sequence and mapping of receptor-binding domain by use of fusion constructs. Infect Immun. 1991 Jan;59(1):261–268. doi: 10.1128/iai.59.1.261-268.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Telen M. J., Hall S. E., Green A. M., Moulds J. J., Rosse W. F. Identification of human erythrocyte blood group antigens on decay-accelerating factor (DAF) and an erythrocyte phenotype negative for DAF. J Exp Med. 1988 Jun 1;167(6):1993–1998. doi: 10.1084/jem.167.6.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Väisänen V., Elo J., Tallgren L. G., Siitonen A., Mäkelä P. H., Svanborg-Edén C., Källenius G., Svenson S. B., Hultberg H., Korhonen T. Mannose-resistant haemagglutination and P antigen recognition are characteristic of Escherichia coli causing primary pyelonephritis. Lancet. 1981 Dec 19;2(8260-61):1366–1369. doi: 10.1016/s0140-6736(81)92796-3. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES