Abstract
CD4 T cells recognize peptide fragments of foreign proteins bound to self class II molecules of the major histocompatibility complex (MHC). Naturally processed peptide fragments bound to MHC class II molecules are peptides of 13–17 amino acids which appear to be precessively truncated from the carboxy terminus, perhaps after binding to the MHC class II molecule. The finding of predominant self peptides has interesting implications for antigen processing and self–non-self discrimination.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Davis, M. M. & Bjorkman, P. J. Nature 334, 395–402 (1988).
Amit, A. G., Mariuzza, R. A., Phillips, S. E. V. & Poljak, R. Science 233, 747–753 (1986).
Zinkernagel, R. M. & Doherty, P. C. Adv. Immun. 27, 51–177 (1979).
Bjorkman, P. J. et al. Nature 329, 506–512 (1987).
Bjorkman, P. J. et al. Nature 329, 512–518 (1987).
Garrett, T. P. J., Saper, M. A., Bjorkman, P. J., Strominger, J. L. & Wiley, D. C. Nature 342, 692–696 (1989).
Morrison, L. A., Lukacher, A. E., Braciale, V. L., Fan, D. P. & Braciale, T. J. J. exp. Med. 163, 903–921 (1986).
Germain, R. N. Nature 322, 687–689 (1986).
Townsend, A. et al. Nature 340, 443–448 (1989).
Rötzschke, O., Falk, K., Wallny, H.-J., Faath, S. & Rammensee, H.-G. Science 249, 283–287 (1990).
Van Bleek, G. M. & Nathanson, S. G. Nature 348, 213–216 (1990).
Rötzschke, O. et al. Nature 348, 253–255 (1990).
Falk, K., Rötzschke, O., Stevanovic, S., Jung, G. & Rammensee, H.-G. Nature 351, 290–296 (1991).
Jardetzky, T., Lane, W., Robinson, R. A., Madden, D. & Wiley, D. C. Nature 353, 326–329 (1991).
Schumacher, T. N. M. et al. Nature 350, 703–706 (1991).
Swain, S. L. Immun. Rev. 74, 129–156 (1983).
Demotz, S., Grey, H. M., Appella, E. & Sette, A. Nature 342, 682–684 (1989).
Srinivasan, H. & Pierce, S. K. Proc. natn. Acad. Sci. U.S.A. 87, 919–922 (1990).
Babbitt, B. P., Allen, P. M., Matsueda, G., Haber, E. & Unanue, E. R. Nature 317, 359–360 (1985).
Watts, T. H., Brian, A. A., Kappler, J. W., Marrack, P. & McConnell, H. M. Proc. natn. Acad. Sci. U.S.A. 81, 7564–7568 (1984).
Kappler, J., White, J., Wegmenn, D., Mustain, E. & Marrack, P. Proc. natn. Acad. Sci. U.S.A. 79, 3604–3607 (1982).
Janeway, C. A. Jr et al. J. Immun. 132, 662–669 (1984).
Lerner, E. A. et al. J. exp. Med. 152, 1085–1101 (1980).
Buus, S., Sette, A., Colon, S. M., Jenis, D. M. & Grey, H. M. Cell 47, 1071–1077 (1986).
Cresswell, P., Blum, J. S., Marks, M. S. & Roche, P. A. Cold Spring Harbor Symp. quant. Biol. 54, 309–318 (1989).
Roche, P. A. & Cresswell, P. Nature 345, 615–618 (1990).
Teyton, L. et al. Nature 348, 39–44 (1990).
Briner, T. J., Guillet, J.-G., Lai, M.-Z., Smith, J. A. & Getter, M. L. in T-cell Receptors (eds Davis, M. M. & Kappler, J. W.) 309–316 (1987).
Murphy, D. B. et al. Nature 338, 765–767 (1989).
Rudensky, A. Y., Rath, S., Preston-Hurlburt, P., Murphy, D. B. & Janeway, C. A. Jr Nature 353, 660–662 (1991).
Möller, G. Immun. Rev., 98, 1–187 (1988).
Blum, J. S. & Cresswell, P. Proc. natn. Acad. Sci. U.S.A. 85, 3975–3980 (1988).
Takahashi, H., Cease, K. B. & Berzofsky, J. A. J. Immun. 142, 2221–2229 (1989).
Falk, K., Rötzschke, O. & Rammensee, H.-G. Nature 348, 248–251 (1990).
Fox, B. S., Carbone, F. R., Germain, R. N., Paterson, Y. & Schwartz, R. H. Nature 331, 538–540 (1988).
Buus, S., Sette, A., Colon, S. M. & Grey, H. M. Science 242, 1045–1047 (1988).
Cease, K. B., Berkower, I., York-Jolley, J. & Berzofsky, J. A. J. exp. Med. 164, 1779–1784 (1986).
Brown, J. H. et al. Nature 332, 845–850 (1988).
Harding, C. V. & Unanue, E. R. Nature 346, 574–576 (1990).
Panina-Bordignon, P., Corradin, G., Roosnek, E., Sette, A. & Lanzavecchia, A. Science 252, 1548–1550 (1991).
Benoist, C. & Mathis, D. Curr. Biol. 1, 143–144 (1991).
Matzinger, P. & Bevan, M. J. Cell. Immun. 29, 1–5 (1977).
vonBoehmer, H., Teh, H. S. & Kisielow, P. Immun. Today 10, 61–66 (1989).
Heath, W. R., Hurd, M. E., Carbone, F. R. & Sherman, L. A. Nature 341, 749–752 (1899).
Stone, K. L. & Williams, K. R. in Macromolecular Sequencing and Synthesis: Selected Methods and Application 7–24 (Liss, New York, 1988).
Pearson, W. R. & Lipman, D. J. Proc. natn. Acad. Sci. U.S.A. 85, 2444–2448 (1988).
Samelson, L. E., Germain, R. N. & Schwartz, R. N. Proc. natn. Acad. Sci. U.S.A. 80, 6972–6976 (1983).
Finnegan, A. et al. J. exp. Med. 164, 897–910 (1986).
Acha-Orbea, H. & McDevitt, H. O. Proc. natn. Acad. Sci. U.S.A. 84, 2435–2439 (1987).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Rudensky, A., Preston-Hurlburt, P., Hong, SC. et al. Sequence analysis of peptides bound to MHC class II molecules. Nature 353, 622–627 (1991). https://doi.org/10.1038/353622a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/353622a0
- Springer Nature Limited
This article is cited by
-
Default polyfunctional T helper 1 response to ample signal 1 alone
Cellular & Molecular Immunology (2021)
-
Ligandomes obtained from different HLA-class II-molecules are homologous for N- and C-terminal residues outside the peptide-binding cleft
Immunogenetics (2019)
-
Contribution of the plasma and lymph Degradome and Peptidome to the MHC Ligandome
Immunogenetics (2019)
-
Ancient features of the MHC class II presentation pathway, and a model for the possible origin of MHC molecules
Immunogenetics (2019)
-
Antigen discovery and specification of immunodominance hierarchies for MHCII-restricted epitopes
Nature Medicine (2018)