H-2 Antigens pp 379-384 | Cite as

Associations Between Class I MHC Antigens and Viral Glycoproteins Detected by Fluorescence Resonance Energy Transfer

  • Jerome H. Hochman
  • Michael Edidin
Part of the NATO ASI Series book series (NSSA, volume 144)

Abstract

Cytotoxic T lymphocytes, CTL, recognize viral antigens of infected cells in the context of the cells’ class I MHC antigens (Zinkernagel and Doherty, 1979). The basis of this MHC restriction is not defined. The weight of the evidence favors recognition of some complex of all or part of viral antigen with the class I antigen. The route of formation of this complex and its stability are still unclear. In some instances, influenza virus infection (Townsend et al., 1984; Yewdell et al., 1985) and SV40 transformation (Gooding and O’Connell, 1983) it is evident that the CTL are primarily directed against internal viral proteins, the nucleocapsid protein of the influenza virus or the T antigen of SV40. This, together with the demonstration that peptides derived from these proteins (Townsend, et al., 1986) can sensitise target cells, strongly implies that these antigens are partly digested, and associated with class I MHC antigens before appearing at the cell surface. Such a mechanism of association parallels that mechanism for the formation of nominal antigen/class II MHC antigen complexes for presentation to helper T cells (Buus et al., 1987; Unanue and Allen, 1987) and unifies our view of antigen presentation to T cells. However, the generality of this scheme is still not clear. Some virus antigens, even the influenza virus nucleocapsid, can be presented to cells under conditions in which processing is blocked (Wraith and Vessey, 1986), suggesting that they associate with class I antigens without internalization and processing.

Keywords

Influenza Virus Fluorescence Resonance Energy Transfer Viral Antigen Influenza Virus Infection Nucleocapsid Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Al-Ahldal, M.N., I. NaKamura and T.D. Flanagan. 1985. J. Virol 54:53-57. Buus, S., A. Sette, S. M. Colon, C. Miles, H. M. Grey. 1987. Science 235:1353-1358.Google Scholar
  2. De Waal, L. P., W. M. Kast, R. W. Melvold and C. J. M. Melief. 1983. J. Immunol 130: 1090 - 1096.PubMedGoogle Scholar
  3. Gooding, L. R. and K. A. O’Connell. 1983. J. Immunol 131:2580. Hochman, J. H. and M. Edidin. 1987. J. Immunol in the press.Google Scholar
  4. Klein, J. 1986. “Natural History of the Major Histocompatibility Complex”. John Wiley and Sons, New York, pp. 455-461.Google Scholar
  5. Kurrle, R., M. Rollinghoff and H. Wagner. 1978. Eur. J. Immunol 8:910-912.Google Scholar
  6. Lakowicz, J. R. 1983. “Principles of Fluorescence Spectroscopy”. Plenum Press, New York and London, ch. 10.Google Scholar
  7. Shapiro, M. W., S. J. Burakoff, B. Benacerraf and R. W. Finberg. 1981. J. Immunol 127: 2571 - 2574.PubMedGoogle Scholar
  8. Stryer, L.. 1978. Ann. Rev. Biochem 47: 819 - 846.PubMedCrossRefGoogle Scholar
  9. Sugamura, K., K. Shimizu, D. A. Zarling and F. H. Bach. 1977. Nature 270:251-253.Google Scholar
  10. Titus, J. A., R. Haugland, S 0. Sharrow and D. M. Segal. 1982.J. Immunol. Methods 50:193-.Google Scholar
  11. Townsend, A. R. M., A. J. McMichael, H. P. Carter, J. A. Huddleston, and G. G. Brownlee. 1984. Cell 39: 13 - 25.Google Scholar
  12. Townsend, A. R. M., J. Rothbard, F. M. Gotch, G. Bandur, D. Wraith and A. J. McMichael. 1986. Cell44: 951 - 968.CrossRefGoogle Scholar
  13. Unanue, E. R. and P. M. Allen. 1987. Science 236:551-557.Google Scholar
  14. Vainstein, A., M. Hershkovitz, S. Israel, S. Rabin and A. Loyter. 1984. Biochim Biophys. Acta773:181-188.Google Scholar
  15. Wraith, D. C., and A. E. Vessey. 1986. Immunology 59: 173 - 180.Google Scholar
  16. Yewdell, J. W., J. R. Bennink, G. L. Smith and B. Moss. 1985.Proc. Natl. Acad. Sci. USA82: 1785 - 1789.CrossRefGoogle Scholar
  17. Zinkernagel, R. and P. Doherty. 1979. Adv. Immunol 27:51-177.Google Scholar
  18. Zinkernagel, R., A. Althage, S. Cooper, G. Kreeb, P. A. Klein, B. Sefton, L.Google Scholar
  19. Flaherty, J. Stimpfling, D. Shreffler and J. Klein. 1978. J. Exp. Med. 148: 592-606.Google Scholar

Copyright information

© Springer Science+Business Media New York 1987

Authors and Affiliations

  • Jerome H. Hochman
    • 1
  • Michael Edidin
    • 1
  1. 1.Department of BiologyThe Johns Hopkins UniversityBaltimoreUSA

Personalised recommendations