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. 1991 Nov;65(11):5673–5679. doi: 10.1128/jvi.65.11.5673-5679.1991

Identification of an immunodominant epitope within the phosphoprotein of rabies virus that is recognized by both class I- and class II-restricted T cells.

J K Larson 1, W H Wunner 1, L Otvos Jr 1, H C Ertl 1
PMCID: PMC250227  PMID: 1717708

Abstract

Immunization of H-2k mice with live rabies virus induces cytolytic T lymphocytes to the phosphoprotein of rabies virus. The antigenic determinant responsible for stimulating this class I-restricted cytolytic response was mapped to 50 amino acids (residues 180 to 229) of the phosphoprotein by using vaccinia virus recombinants expressing either the full-length phosphoprotein or C-terminal truncations of the phosphoprotein. The epitope was more finely mapped to residues 191 to 206 by using synthetic peptides. Several CD4+, class II-restricted T-cell lines were isolated from splenocytes of H-2k mice immunized with the vaccinia virus-rabies virus phosphoprotein recombinant virus. These lines were specifically stimulated by the phosphoprotein, and in addition, each line proliferated and released lymphokines in response to the same synthetic peptide shown to stimulate phosphoprotein-specific, class I-restricted cytolytic T cells.

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Selected References

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

  1. Celis E., Ou D., Otvos L., Jr Recognition of hepatitis B surface antigen by human T lymphocytes. Proliferative and cytotoxic responses to a major antigenic determinant defined by synthetic peptides. J Immunol. 1988 Mar 15;140(6):1808–1815. [PubMed] [Google Scholar]
  2. Chen C., Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol. 1987 Aug;7(8):2745–2752. doi: 10.1128/mcb.7.8.2745. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. DeLisi C., Berzofsky J. A. T-cell antigenic sites tend to be amphipathic structures. Proc Natl Acad Sci U S A. 1985 Oct;82(20):7048–7052. doi: 10.1073/pnas.82.20.7048. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dietzschold B., Lafon M., Wang H., Otvos L., Jr, Celis E., Wunner W. H., Koprowski H. Localization and immunological characterization of antigenic domains of the rabies virus internal N and NS proteins. Virus Res. 1987 Aug;8(2):103–125. doi: 10.1016/0168-1702(87)90023-2. [DOI] [PubMed] [Google Scholar]
  5. Dietzschold B., Wang H. H., Rupprecht C. E., Celis E., Tollis M., Ertl H., Heber-Katz E., Koprowski H. Induction of protective immunity against rabies by immunization with rabies virus ribonucleoprotein. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9165–9169. doi: 10.1073/pnas.84.24.9165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ertl H. C., Dietzschold B., Gore M., Otvos L., Jr, Larson J. K., Wunner W. H., Koprowski H. Induction of rabies virus-specific T-helper cells by synthetic peptides that carry dominant T-helper cell epitopes of the viral ribonucleoprotein. J Virol. 1989 Jul;63(7):2885–2892. doi: 10.1128/jvi.63.7.2885-2892.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ertl H. C., Dietzschold B., Otvos L., Jr T helper cell epitope of rabies virus nucleoprotein defined by tri- and tetrapeptides. Eur J Immunol. 1991 Jan;21(1):1–10. doi: 10.1002/eji.1830210102. [DOI] [PubMed] [Google Scholar]
  8. Gao X. M., Liew F. Y., Tite J. P. Identification and characterization of T helper epitopes in the nucleoprotein of influenza A virus. J Immunol. 1989 Nov 1;143(9):3007–3014. [PubMed] [Google Scholar]
  9. Houghten R. A. General method for the rapid solid-phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual amino acids. Proc Natl Acad Sci U S A. 1985 Aug;82(15):5131–5135. doi: 10.1073/pnas.82.15.5131. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kawano H., Mifune K., Ohuchi M., Mannen K., Cho S., Hiramatsu K., Shichijo A. Protection against rabies in mice by a cytotoxic T cell clone recognizing the glycoprotein of rabies virus. J Gen Virol. 1990 Feb;71(Pt 2):281–287. doi: 10.1099/0022-1317-71-2-281. [DOI] [PubMed] [Google Scholar]
  11. Knowles B. B., Koncar M., Pfizenmaier K., Solter D., Aden D. P., Trinchieri G. Genetic control of the cytotoxic T cell response to SV40 tumor-associated specific antigen. J Immunol. 1979 May;122(5):1798–1806. [PubMed] [Google Scholar]
  12. Larson J. K., Wunner W. H. Nucleotide and deduced amino acid sequences of the nominal nonstructural phosphoprotein of the ERA, PM and CVS-11 strains of rabies virus. Nucleic Acids Res. 1990 Dec 11;18(23):7172–7172. doi: 10.1093/nar/18.23.7172. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Margalit H., Spouge J. L., Cornette J. L., Cease K. B., Delisi C., Berzofsky J. A. Prediction of immunodominant helper T cell antigenic sites from the primary sequence. J Immunol. 1987 Apr 1;138(7):2213–2229. [PubMed] [Google Scholar]
  14. Milich D. R. Probing T cell antigen recognition: use of synthetic peptides. Pept Res. 1990 Mar-Apr;3(2):85–96. [PubMed] [Google Scholar]
  15. Morrison L. A., Lukacher A. E., Braciale V. L., Fan D. P., Braciale T. J. Differences in antigen presentation to MHC class I-and class II-restricted influenza virus-specific cytolytic T lymphocyte clones. J Exp Med. 1986 Apr 1;163(4):903–921. doi: 10.1084/jem.163.4.903. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Perkins D. L., Lai M. Z., Smith J. A., Gefter M. L. Identical peptides recognized by MHC class I- and II-restricted T cells. J Exp Med. 1989 Jul 1;170(1):279–289. doi: 10.1084/jem.170.1.279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Pierce C. W., Kapp J. A., Benacerraf B. Regulation by the H-2 gene complex of macrophage-lymphoid cell interactions in secondary antibody responses in vitro. J Exp Med. 1976 Aug 1;144(2):371–381. doi: 10.1084/jem.144.2.371. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Reddehase M. J., Rothbard J. B., Koszinowski U. H. A pentapeptide as minimal antigenic determinant for MHC class I-restricted T lymphocytes. Nature. 1989 Feb 16;337(6208):651–653. doi: 10.1038/337651a0. [DOI] [PubMed] [Google Scholar]
  19. Rothbard J. B., Taylor W. R. A sequence pattern common to T cell epitopes. EMBO J. 1988 Jan;7(1):93–100. doi: 10.1002/j.1460-2075.1988.tb02787.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Schwartz R. H., Fox B. S., Fraga E., Chen C., Singh B. The T lymphocyte response to cytochrome c. V. Determination of the minimal peptide size required for stimulation of T cell clones and assessment of the contribution of each residue beyond this size to antigenic potency. J Immunol. 1985 Oct;135(4):2598–2608. [PubMed] [Google Scholar]
  22. Sikes R. K., Cleary W. F., Koprowski H., Wiktor T. J., Kaplan M. M. Effective protection of monkeys against death from street virus by post-exposure administration of tissue-culture rabies vaccine. Bull World Health Organ. 1971;45(1):1–11. [PMC free article] [PubMed] [Google Scholar]
  23. Takahashi H., Cohen J., Hosmalin A., Cease K. B., Houghten R., Cornette J. L., DeLisi C., Moss B., Germain R. N., Berzofsky J. A. An immunodominant epitope of the human immunodeficiency virus envelope glycoprotein gp160 recognized by class I major histocompatibility complex molecule-restricted murine cytotoxic T lymphocytes. Proc Natl Acad Sci U S A. 1988 May;85(9):3105–3109. doi: 10.1073/pnas.85.9.3105. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Tanaka Y., Tevethia M. J., Kalderon D., Smith A. E., Tevethia S. S. Clustering of antigenic sites recognized by cytotoxic T lymphocyte clones in the amino terminal half of SV40 T antigen. Virology. 1988 Feb;162(2):427–436. doi: 10.1016/0042-6822(88)90483-7. [DOI] [PubMed] [Google Scholar]
  25. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Townsend A. R., Gotch F. M., Davey J. Cytotoxic T cells recognize fragments of the influenza nucleoprotein. Cell. 1985 Sep;42(2):457–467. doi: 10.1016/0092-8674(85)90103-5. [DOI] [PubMed] [Google Scholar]
  27. Whitton J. L., Gebhard J. R., Lewicki H., Tishon A., Oldstone M. B. Molecular definition of a major cytotoxic T-lymphocyte epitope in the glycoprotein of lymphocytic choriomeningitis virus. J Virol. 1988 Mar;62(3):687–695. doi: 10.1128/jvi.62.3.687-695.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Wiktor T. J., Dietzschold B., Leamnson R. N., Koprowski H. Induction and biological properties of defective interfering particles of rabies virus. J Virol. 1977 Feb;21(2):626–635. doi: 10.1128/jvi.21.2.626-635.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Wiktor T. J., Macfarlan R. I., Reagan K. J., Dietzschold B., Curtis P. J., Wunner W. H., Kieny M. P., Lathe R., Lecocq J. P., Mackett M. Protection from rabies by a vaccinia virus recombinant containing the rabies virus glycoprotein gene. Proc Natl Acad Sci U S A. 1984 Nov;81(22):7194–7198. doi: 10.1073/pnas.81.22.7194. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Zinkernagel R. M., Doherty P. C. Restriction of in vitro T cell-mediated cytotoxicity in lymphocytic choriomeningitis within a syngeneic or semiallogeneic system. Nature. 1974 Apr 19;248(5450):701–702. doi: 10.1038/248701a0. [DOI] [PubMed] [Google Scholar]

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