Skip to main content
Infection and Immunity logoLink to Infection and Immunity
. 1982 Jul;37(1):250–254. doi: 10.1128/iai.37.1.250-254.1982

Immunological cross-reactivity in the absence of DNA homology between Pseudomonas toxin A and diphtheria toxin.

J C Sadoff, G A Buck, B H Iglewski, M J Bjorn, N B Groman
PMCID: PMC347520  PMID: 6179878

Abstract

The immunodominant determinant of Pseudomonas toxin A was shown to cross-react with a normally inaccessible determinant in fragment A of diphtheria toxin. Trypsin-treated diphtheria toxin and fragment A of diphtheria toxin inhibited binding of toxin A antibody to whole toxin A, whereas whole diphtheria toxin did not inhibit this reaction. However, even at the lowest stringency no hybridization was detected between diphtheria tox probe and Pseudomonas aeruginosa DNA.

Full text

PDF
250

Images in this article

Selected References

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

  1. Bjorn M. J., Pavlovskis O. R., Thompson M. R., Iglewski B. H. Production of exoenzyme S during Pseudomonas aeruginosa infections of burned mice. Infect Immun. 1979 Jun;24(3):837–842. doi: 10.1128/iai.24.3.837-842.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Buck G. A., Groman N. B. Identification of deoxyribonucleic acid restriction fragments of beta-converting corynebacteriophages that carry the gene for diphtheria toxin. J Bacteriol. 1981 Oct;148(1):153–162. doi: 10.1128/jb.148.1.153-162.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Buck G. A., Groman N. B. Physical mapping of beta-converting and gamma-nonconverting corynebacteriophage genomes. J Bacteriol. 1981 Oct;148(1):131–142. doi: 10.1128/jb.148.1.131-142.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Buck G., Groman N., Falkow S. Relationship between beta converting and gamma non-converting corynebacteriophage DNA. Nature. 1978 Feb 16;271(5646):683–685. doi: 10.1038/271683a0. [DOI] [PubMed] [Google Scholar]
  5. Chung D. W., Collier R. J. Enzymatically active peptide from the adenosine diphosphate-ribosylating toxin of Pseudomonas aeruginosa. Infect Immun. 1977 Jun;16(3):832–841. doi: 10.1128/iai.16.3.832-841.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Collier R. J. Diphtheria toxin: mode of action and structure. Bacteriol Rev. 1975 Mar;39(1):54–85. doi: 10.1128/br.39.1.54-85.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Collier R. J., Kandel J. Structure and activity of diphtheria toxin. I. Thiol-dependent dissociation of a fraction of toxin into enzymically active and inactive fragments. J Biol Chem. 1971 Mar 10;246(5):1496–1503. [PubMed] [Google Scholar]
  8. Cryz S. J., Jr, Friedman R. L., Pavlovskis O. R., Iglewski B. H. Effect of formalin toxoiding on Pseudomonas aeruginosa toxin A: biological, chemical, and immunochemical studies. Infect Immun. 1981 May;32(2):759–768. doi: 10.1128/iai.32.2.759-768.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Holmes R. K., Baine W. B., Vasil M. L. Quantitative measurements of cholera enterotoxin in cultures of toxinogenic wild-type and nontoxinogenic mutant strains of Vibrio cholerae by using a sensitive and specific reversed passive hemagglutination assay for cholera enerotoxin. Infect Immun. 1978 Jan;19(1):101–106. doi: 10.1128/iai.19.1.101-106.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Holmgren J. Comparison of the tissue receptors for Vibrio cholerae and Escherichia coli enterotoxins by means of gangliosides and natural cholera toxoid. Infect Immun. 1973 Dec;8(6):851–859. doi: 10.1128/iai.8.6.851-859.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Howley P. M., Israel M. A., Law M. F., Martin M. A. A rapid method for detecting and mapping homology between heterologous DNAs. Evaluation of polyomavirus genomes. J Biol Chem. 1979 Jun 10;254(11):4876–4883. [PubMed] [Google Scholar]
  12. Iglewski B. H., Kabat D. NAD-dependent inhibition of protein synthesis by Pseudomonas aeruginosa toxin,. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2284–2288. doi: 10.1073/pnas.72.6.2284. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Iglewski B. H., Liu P. V., Kabat D. Mechanism of action of Pseudomonas aeruginosa exotoxin Aiadenosine diphosphate-ribosylation of mammalian elongation factor 2 in vitro and in vivo. Infect Immun. 1977 Jan;15(1):138–144. doi: 10.1128/iai.15.1.138-144.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Iglewski B. H., Sadoff J. C. Toxin inhibitors of protein synthesis: production, purification, and assay of Pseudomonas aeruginosa toxin A. Methods Enzymol. 1979;60:780–793. doi: 10.1016/s0076-6879(79)60071-x. [DOI] [PubMed] [Google Scholar]
  15. Leppla S. H. Large-scale purification and characterization of the exotoxin of Pseudomonas aeruginosa. Infect Immun. 1976 Oct;14(4):1077–1086. doi: 10.1128/iai.14.4.1077-1086.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lightfoot H. N., Iglewski B. H. Synthesis of diphtheria toxin in E. coli cell-free lysate. Biochem Biophys Res Commun. 1974 Jan 23;56(2):351–357. doi: 10.1016/0006-291x(74)90849-3. [DOI] [PubMed] [Google Scholar]
  17. Middlebrook J. L., Dorland R. B. Response of cultured mammalian cells to the exotoxins of Pseudomonas aeruginosa and Corynebacterium diphtheriae: differential cytotoxicity. Can J Microbiol. 1977 Feb;23(2):183–189. doi: 10.1139/m77-026. [DOI] [PubMed] [Google Scholar]
  18. Moseley S. L., Falkow S. Nucleotide sequence homology between the heat-labile enterotoxin gene of Escherichia coli and Vibrio cholerae deoxyribonucleic acid. J Bacteriol. 1980 Oct;144(1):444–446. doi: 10.1128/jb.144.1.444-446.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Pappenheimer A. M., Jr, Uchida T., Harper A. A. An immunological study of the diphtheria toxin molecule. Immunochemistry. 1972 Sep;9(9):891–906. doi: 10.1016/0019-2791(72)90163-2. [DOI] [PubMed] [Google Scholar]
  20. Pemberton J. M. Size of the chromosome of Pseudomonas aeruginosa PAO. J Bacteriol. 1974 Sep;119(3):748–752. doi: 10.1128/jb.119.3.748-752.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Rittenberg M. B., Pinney C. T., Jr, Iglewski B. H. Antigenic relationships on the diphtheria toxin molecule: antitoxin versus antitoxoid. Infect Immun. 1976 Jul;14(1):122–128. doi: 10.1128/iai.14.1.122-128.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Zollinger W. D., Dalrymple J. M., Artenstein M. S. Analysis of parameters affecting the solid phase radioimmunoassay quantitation of antibody to meningococcal antigens. J Immunol. 1976 Nov;117(5 PT2):1788–1798. [PubMed] [Google Scholar]
  23. Zollinger W. D., Mandrell R. E. Outer-membrane protein and lipopolysaccharide serotyping of Neisseria meningitidis by inhibition of a solid-phase radioimmunoassay. Infect Immun. 1977 Nov;18(2):424–433. doi: 10.1128/iai.18.2.424-433.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES