Skip to main content
PMC home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1984 Nov 1;160(5):1338–1349. doi: 10.1084/jem.160.5.1338

Identification of the principal T lymphocyte-stimulating antigens of Pseudomonas aeruginosa

PMCID: PMC2187495  PMID: 6208308

Abstract

To aid in understanding the role of cellular immunity in limiting Pseudomonas aeruginosa infections, we have identified some of the principal antigens of the organism that are recognized by human T cells. Clones of T cells were selected in such a manner that they would provide information not only about the identity of Pseudomonas antigens, but also the T cell repertoires of immune donors. Most clones were found to be specific for Pseudomonas alkaline protease (AP). Such clones could be physically isolated by selecting with crude Pseudomonas antigens or purified AP. In either case, their fine specificities were the same when tested against a panel of Pseudomonas antigens. The conclusion that AP is the principal immunogen for many donors was confirmed by measuring the absolute frequencies of proliferating T cells committed to AP and all other Pseudomonas antigens. Frequencies of AP-specific clones (1.5-2.7 X 10(-5] were comparable to those from the same donors that were specific for all secreted Pseudomonas antigens (1.3-6.0 X 10(-5]. These results provide a model system for studying human T cell-mediated immunity to bacteria by identifying discrete antigens and measuring the repertoire diversities of cells responding to them.

Full Text

The Full Text of this article is available as a PDF (719.8 KB).

Selected References

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

  1. Cross A. S., Sadoff J. C., Iglewski B. H., Sokol P. A. Evidence for the role of toxin A in the pathogenesis of infection with Pseudomonas aeruginosa in humans. J Infect Dis. 1980 Oct;142(4):538–546. doi: 10.1093/infdis/142.4.538. [DOI] [PubMed] [Google Scholar]
  2. Ford D., Burger D. Precursor frequency of antigen-specific T cells: effects of sensitization in vivo and in vitro. Cell Immunol. 1983 Jul 15;79(2):334–344. doi: 10.1016/0008-8749(83)90075-8. [DOI] [PubMed] [Google Scholar]
  3. Gebel H. M., Scott J. R., Parvin C. A., Rodey G. E. In vitro immunization to KLH. II. Limiting dilution analysis of antigen-reactive cells in primary and secondary culture. J Immunol. 1983 Jan;130(1):29–32. [PubMed] [Google Scholar]
  4. Holloway B. W., Krishnapillai V., Morgan A. F. Chromosomal genetics of Pseudomonas. Microbiol Rev. 1979 Mar;43(1):73–102. doi: 10.1128/mr.43.1.73-102.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Howe T. R., Iglewski B. H. Isolation and characterization of alkaline protease-deficient mutants of Pseudomonas aeruginosa in vitro and in a mouse eye model. Infect Immun. 1984 Mar;43(3):1058–1063. doi: 10.1128/iai.43.3.1058-1063.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Iglewski B. H., Burns R. P., Gipson I. K. Pathogenesis of corneal damage from pseudomonas exotoxin A. Invest Ophthalmol Vis Sci. 1977 Jan;16(1):73–76. [PubMed] [Google Scholar]
  7. 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]
  8. Kawaharajo K., Abe C., Homma J. Y., Kawano M., Goto E. Corneal ulcers caused by protease and elastase from Pseudomonas aeruginosa. Jpn J Exp Med. 1974 Oct;44(5):435–442. [PubMed] [Google Scholar]
  9. Kawaharajo K., Abe C., Homma J. Y., Kawano M., Goto E. Corneal ulcers caused by protease and elastase from Pseudomonas aeruginosa. Jpn J Exp Med. 1974 Oct;44(5):435–442. [PubMed] [Google Scholar]
  10. Kawaharajo K., Homma J. Y. Pathogenesis of the mouse keratitis produced with Pseudomonas aeruginosa. Jpn J Exp Med. 1975 Dec;45(6):515–524. [PubMed] [Google Scholar]
  11. Kreger A. S., Gray L. D. Purification of Pseudomonas aeruginosa proteases and microscopic characterization of pseudomonal protease-induced rabbit corneal damage. Infect Immun. 1978 Feb;19(2):630–648. doi: 10.1128/iai.19.2.630-648.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kreger A. S., Griffin O. K. Physicochemical fractionation of extracellular cornea-damaging proteases of Pseudomonas aeruginosa. Infect Immun. 1974 May;9(5):828–834. doi: 10.1128/iai.9.5.828-834.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lamb J. R., Eckels D. D., Phelan M., Lake P., Woody J. N. Antigen-specific human T lymphocyte clones: viral antigen specificity of influenza virus-immune clones. J Immunol. 1982 Mar;128(3):1428–1432. [PubMed] [Google Scholar]
  14. Liu P. V., Hsieh H. Exotoxins of Pseudomonas aeruginosa. 3. Characteristics of antitoxin A. J Infect Dis. 1973 Oct;128(4):520–526. doi: 10.1093/infdis/128.4.520. [DOI] [PubMed] [Google Scholar]
  15. MORIHARA K. PRODUCTION OF ELASTASE AND PROTEINASE BY PSEUDOMONAS AERUGINOSA. J Bacteriol. 1964 Sep;88:745–757. doi: 10.1128/jb.88.3.745-757.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ohman D. E., Burns R. P., Iglewski B. H. Corneal infections in mice with toxin A and elastase mutants of Pseudomonas aeruginosa. J Infect Dis. 1980 Oct;142(4):547–555. doi: 10.1093/infdis/142.4.547. [DOI] [PubMed] [Google Scholar]
  17. Ohman D. E., Cryz S. J., Iglewski B. H. Isolation and characterization of Pseudomonas aeruginosa PAO mutant that produces altered elastase. J Bacteriol. 1980 Jun;142(3):836–842. doi: 10.1128/jb.142.3.836-842.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Ohman D. E., Sadoff J. C., Iglewski B. H. Toxin A-deficient mutants of Pseudomonas aeruginosa PA103: isolation and characterization. Infect Immun. 1980 Jun;28(3):899–908. doi: 10.1128/iai.28.3.899-908.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Pier G. B., Markham R. B. Induction in mice of cell-mediated immunity to Pseudomonas aeruginosa by high molecular weight polysaccharide and vinblastine. J Immunol. 1982 May;128(5):2121–2125. [PubMed] [Google Scholar]
  20. 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]
  21. Pollack M., Young L. S. Protective activity of antibodies to exotoxin A and lipopolysaccharide at the onset of Pseudomonas aeruginosa septicemia in man. J Clin Invest. 1979 Feb;63(2):276–286. doi: 10.1172/JCI109300. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Rinderknecht H., Geokas M. C., Silverman P., Haverback B. J. A new ultrasensitive method for the determination of proteolytic activity. Clin Chim Acta. 1968 Aug;21(2):197–203. doi: 10.1016/0009-8981(68)90127-7. [DOI] [PubMed] [Google Scholar]
  23. Sohnle P. G., Collins-Lech C. Lymphocyte transformation and the number of antigen-responsive cells in humans. J Immunol. 1981 Aug;127(2):612–615. [PubMed] [Google Scholar]
  24. Sorensen R. U., Stern R. C., Polmar S. H. Cellular immunity to bacteria: impairment of in vitro lymphocyte responses to Pseudomonas aeruginosa in cystic fibrosis patients. Infect Immun. 1977 Dec;18(3):735–740. doi: 10.1128/iai.18.3.735-740.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Sorensen R. U., Stern R. C., Polmar S. H. Lymphocyte responsiveness to Pseudomonas aeruginosa in cystic fibrosis: Relationship to status of pulmonary disease in sibling pairs. J Pediatr. 1978 Aug;93(2):201–205. doi: 10.1016/s0022-3476(78)80496-x. [DOI] [PubMed] [Google Scholar]
  26. Yem A. W., Parmely M. J. Modulation of Ia-like antigen expression and antigen-presenting activity of human monocytes by endotoxin and zymosan A. J Immunol. 1981 Dec;127(6):2245–2251. [PubMed] [Google Scholar]
  27. van Oers M. H., Pinkster J., Zeijlemaker W. P. Quantification of antigen-reactive cells among human T lymphocytes. Eur J Immunol. 1978 Jul;8(7):477–484. doi: 10.1002/eji.1830080706. [DOI] [PubMed] [Google Scholar]

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

RESOURCES