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Infection and Immunity logoLink to Infection and Immunity
. 1977 Jun;16(3):832–841. doi: 10.1128/iai.16.3.832-841.1977

Enzymatically active peptide from the adenosine diphosphate-ribosylating toxin of Pseudomonas aeruginosa.

D W Chung, R J Collier
PMCID: PMC421038  PMID: 19354

Abstract

A nontoxic peptide (molecular weight, 26,000), which is active in catalyzing the adenosine diphosphate (ADP)-ribosylation of elongation factor 2, has been isolated from the culture supernatant of Pseudomonas aeruginosa strain 103 in stationary phase. Like fragment A from diphtheria toxin, the active peptide catalyzed the hydrolysis of nicotinamide adenine dinucleotide as well as the ADP-ribosylation of elongation factor 2 and showed similarities to fragment A in specific activity, kinetic constants, pH optimum, and ionic sensitivity. These results provide strong evidence for a high degree of homology in the structures of their active sites. That the peptide is not identical to fragment A is shown by the fact that it was not neutralized by fragment A-specific antiserum and was different in amino acid composition and pH and thermal labilities. Although definitive evidence is lacking, there are data suggesting that this peptide is a proteolytic fragment from the ADP-ribosylating toxin (exotoxin A; molecular weight, 66,000) produced by the same strain of P. aeruginosa.

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Selected References

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  1. Birnboim H. C. Optimal conditions for counting of precipitated 3H-RNA on glass-fiber filters. Anal Biochem. 1970 Sep;37(1):178–182. doi: 10.1016/0003-2697(70)90275-7. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. 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]
  4. DeLange R. J., Drazin R. E., Collier R. J. Amino-acid sequence of fragment A, an enzymically active fragment from diphtheria toxin. Proc Natl Acad Sci U S A. 1976 Jan;73(1):69–72. doi: 10.1073/pnas.73.1.69. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. Legocki A. B., Marcus A. Polypeptide synthesis in extracts of wheat germ. Resolution and partial purification of the soluble transfer factors. J Biol Chem. 1970 Jun 10;245(11):2814–2818. [PubMed] [Google Scholar]
  7. 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]
  8. Liu P. V. Exotoxins of Pseudomonas aeruginosa. I. Factors that influence the production of exotoxin A. J Infect Dis. 1973 Oct;128(4):506–513. doi: 10.1093/infdis/128.4.506. [DOI] [PubMed] [Google Scholar]
  9. Liu P. V. The roles of various fractions of Pseudomonas aeruginosa in its pathogenesis. 3. Identity of the lethal toxins produced in vitro and in vivo. J Infect Dis. 1966 Oct;116(4):481–489. doi: 10.1093/infdis/116.4.481. [DOI] [PubMed] [Google Scholar]
  10. Liu P. V., Yoshii S., Hsieh H. Exotoxins of Pseudomonas aeruginosa. II. Concentration, purification, and characterization of exotoxin A. J Infect Dis. 1973 Oct;128(4):514–519. doi: 10.1093/infdis/128.4.514. [DOI] [PubMed] [Google Scholar]
  11. Pappenheimer A. M., Jr, Gill D. M. Diphtheria. Science. 1973 Oct 26;182(4110):353–358. doi: 10.1126/science.182.4110.353. [DOI] [PubMed] [Google Scholar]
  12. Pavlovskis O. R., Gordon F. B. Pseudomonas aeruginosa exotoxin: effect on cell cultures. J Infect Dis. 1972 Jun;125(6):631–636. doi: 10.1093/infdis/125.6.631. [DOI] [PubMed] [Google Scholar]
  13. Pavlovskis O. R., Shackelford A. H. Pseudomonas aeruginosa exotoxin in mice: localization and effect on protein synthesis. Infect Immun. 1974 Mar;9(3):540–546. doi: 10.1128/iai.9.3.540-546.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Reid M. S., Bieleski R. L. A simple apparatus for vertical flat-sheet polyacrylamide gel electrophoresis. Anal Biochem. 1968 Mar;22(3):374–381. doi: 10.1016/0003-2697(68)90278-9. [DOI] [PubMed] [Google Scholar]
  15. Seal S. N., Bewley J. D., Marcus A. Protein chain initiation in wheat embryo. Resolution and function of the soluble factors. J Biol Chem. 1972 Apr 25;247(8):2592–2597. [PubMed] [Google Scholar]

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