Abstract
The data presented indicate that one of the primary actions of Pseudomonas aeruginosa exotoxin during experimental infection is the inactivation of elongation factor 2 (EF-2) in various mouse organs. Organs from mice infected with the toxigenic P. aeruginosa strain PA103 contained considerably less EF-2 activity than did organs from uninfected controls. Whereas EF-2 activity was reduced in all organs examined from PA103-infected animals, the largest decrease was observed in the liver, where the active EF-2 levels were reduced by 70 to 90%. In addition, consistent inhibition of protein synthesis in livers but not in other organs was observed in mice infected with the toxigenic PA103 strain. Treatment of mice with antitoxin before infection with strain PA103 prevented inactivation of EF-2. When mice were infected with lethal doses of the nontoxigenic P. aeruginosa WR5 strain, tissue EF-2 levels were not markedly reduced below those derived from uninfected control animals.
Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bjorn M. J., Vasil M. L., Sadoff J. C., Iglewski B. H. Incidence of exotoxin production by Pseudomonas species. Infect Immun. 1977 Apr;16(1):362–366. doi: 10.1128/iai.16.1.362-366.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Callahan L. T., 3rd Pseudomonas aeruginosa exotoxin: purification by preparative polyacrylamide gel electrophoresis and the development of a highly specific antitoxin serum. Infect Immun. 1976 Jul;14(1):55–61. doi: 10.1128/iai.14.1.55-61.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Callahan L. T., 3rd Purification and characterization of Pseudomonas aeruginosa exotoxin. Infect Immun. 1974 Jan;9(1):113–118. doi: 10.1128/iai.9.1.113-118.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gill D. M., Dinius L. L. The elongation factor 2 content of mammalian cells. Assay method and relation to ribosome number. J Biol Chem. 1973 Jan 25;248(2):654–658. [PubMed] [Google Scholar]
- Gill D. M., Pappenheimer A. M., Jr, Baseman J. B. Studies on transferase II using diphtheria toxin. Cold Spring Harb Symp Quant Biol. 1969;34:595–602. doi: 10.1101/sqb.1969.034.01.068. [DOI] [PubMed] [Google Scholar]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- Pavlovskis O. R., Pollack M., Callahan L. T., 3rd, Iglewski B. H. Passive protection by antitoxin in experimental Pseudomonas aeruginosa burn infections. Infect Immun. 1977 Dec;18(3):596–602. doi: 10.1128/iai.18.3.596-602.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Pollack M., Callahan L. T., 3rd, Taylor N. S. Neutralizing antibody to Pseudomonas aeruginosa exotoxin in human sera: evidence for in vivo toxin production during infection. Infect Immun. 1976 Oct;14(4):942–947. doi: 10.1128/iai.14.4.942-947.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pollack M., Taylor N. S. Serum antibody to Pseudomonas aeruginosa exotoxin measured by a passive hemagglutination assay. J Clin Microbiol. 1977 Jul;6(1):58–61. doi: 10.1128/jcm.6.1.58-61.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Saelinger C. B., Snell K., Holder I. A. Experimental studies on the pathogenesis of infections due to Pseudomonas aeruginosa: direct evidence for toxin production during Pseudomonas infection of burned skin tissues. J Infect Dis. 1977 Oct;136(4):555–561. doi: 10.1093/infdis/136.4.555. [DOI] [PubMed] [Google Scholar]
- Stieritz D. D., Holder I. A. Experimental studies of the pathogenesis of infections due to Pseudomonas aeruginosa: description of a burned mouse model. J Infect Dis. 1975 Jun;131(6):688–691. doi: 10.1093/infdis/131.6.688. [DOI] [PubMed] [Google Scholar]
- Vasil M. L., Liu P. V., Iglewski B. H. Temperature-dependent inactivating factor of Pseudomonas aeruginosa exotoxin A. Infect Immun. 1976 May;13(5):1467–1472. doi: 10.1128/iai.13.5.1467-1472.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]