Abstract
A mouse major histocompatibility antigen (H–2) gene, encoding a novel H–2Ld molecule lacking its intracytoplasmic domain, has been constructed and introduced into mouse L-cells. The novel H–2 molecule is found on the surface of the transfected cells at the same level as L-cells transfected with the native H–2Ld gene. Allo- and influenza-specific cytotoxic T lymphocytes can recognize the truncated H–2 gene product nearly as efficiently as the normal H–2Ld gene product. However, vesicular stomatitis virus-specific cytotoxic T lymphocytes recognize the truncated H–2Ld molecule less efficiently than the complete H–2Ld product. The rate of capping of the truncated H–2Ld molecule was investigated and found to be the same as that of the complete H–2Ld gene product.
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References
Klein, J. Biology of the Mouse Histocompatibility Complex (Springer, Berlin, 1975).
Snell, G. D., Dausset, J. & Nathenson, S. G. Histocompatibility (Academic, New York, 1976).
Steinmetz, M. S. et al. Cell 25, 683–692 (1981).
Evans, G. A., Margulies, D. H., Ozato, K., Camerini-Otero, R. D. & Seidman, J. G. Proc. natn. Acad. Sci. U.S.A. 79, 1994–1998 (1982).
Moore, K. W., Sher, B. T., San, Y. H., Earle, K. A. & Hood, L. Science 215, 679–682 (1982).
Doherty, P. C. & Zinkernagel, R. M. J. exp. Med. 191, 502–507 (1975).
Zinkernagel, R. M. & Doherty, P. C. Adv. Immun. 27, 51–177 (1979).
Goodenow, P. S. et al. Science 215, 677–679 (1982).
Margulies, D. H. et al. J. Immun. 130, 463–470 (1983).
Woodward, J. G. et al. Proc. natn. Acad. Sci. U.S.A. 79, 3613–3617 (1982).
Mellor, A. L. et al. Nature 228, 529–534 (1982).
Evans, G. A., Margulies, D. H., Shykind, B., Seidman, J. G. & Ozato, K. Nature 300, 755–757 (1982).
Ozato, K., Evans, G. A., Shykind, B., Margulies, D. H. & Seidman, J. G. Proc. natn. Acad. Sci. U.S.A. 80, 2040–2043 (1983).
Reiss, C. S., Evans, G. A., Margulies, D. H., Seidman, J. G. & Burakoff, S. J. Proc. natn. Acad. Sci. U.S.A. 80, 2709–2712 (1983).
Braun, J. & Unanue, E. R. Fedn Proc. 42, 2996–2951 (1983).
Choi, E., McIntyre, K., Germain, R. N. & Seidman, J. G. Science 221, 283–286 (1983).
Graham, F. L. & van der Eb, A. J. Virology 52, 546–553 (1973).
Wigler, M. et al. Proc. natn. Acad. Sci. U.S.A. 76, 1373–1377 (1979).
Ozato, K., Hansen, T. H. & Sachs, D. H. J. Immun. 125, 2973–2977 (1980).
Ozato, K. & Sachs, D. H. J. Immun. 126, 317–321 (1981).
Robinson, R. R., Germain, R. N., McKean, D. J., Mescher, M. & Seidman, J. G. J. Immun. 131, 2025–2031 (1983).
Taylor, R. B., Duffus, R. W., Ruff, M. & de Petris, S. Nature new Biol. 233, 225–229 (1971).
Loor, F. L. Eur. J. Immun. 4, 210–215 (1974).
Nicholson, A. L. Biochim. biophys. Acta 457, 57–108 (1977).
Flanagan, J. & Koch, G. L. E. Nature 273, 278–281 (1978).
Bubbers, J. E., Chew, S. & Lilly, F. J. exp. Med. 147, 340 (1979).
Kirst, S., Ostberg, L., Persson, H., Philipson, L. & Peterson, P. A. Proc. natn. Acad. Sci. U.S.A. 75, 5674–5678 (1978).
Signas, L., Katze, M. G., Persson, H. & Philipson, L. Nature 299, 175–178 (1982).
Ciaverra, R. & Forman, J. F. Immun. Rev. 50, 73–78 (1981).
Geiger, B., Rosenthal, K. L., Klein, J., Zinkernagel, R. M. & Singer, J. Proc. natn. Acad. Sci. U.S.A. 76, 4603–4607 (1979).
Hackett, L. J. & Askonas, B. A. Immunology 45, 431–436 (1982).
Maniatis, T., Fritisch, E. F. & Sambrook, J. Molecular Cloning (Cold Spring Harbor Laboratory, New York, 1982).
Dagert, M. & Ehrlich, S. D. Gene 6, 23–28 (1979).
Holmes, D. S. & Grigley, M. Analyt. Biochem. 114, 193–197 (1981).
Haustein, D., Marchalonis, J. J. & Harris, A. W. Biochemistry 14, 1826–1829 (1975).
Borst, J., Prendiville, M. A. & Terhorst, C. J. Immun. 128, 1560–1565 (1982).
Laemmli, U. K. Nature 227, 680–685 (1970).
Sanger, F., Coulson, A. R., Barrell, B. G., Smith, A. J. H. & Roe, B. A. J. molec. Biol. 143, 161–171 (1980).
Ley, T. J., Anagnon, N. P., Pepe, G. & Nienhuis, A. W. Proc. natn. Acad. Sci. U.S.A. 79, 9775–9779 (1982).
Chirgwin, J. M., Prsybyla, G., MacDonald, R. J. & Rutter, W. J. Biochemistry 18, 5294–5299 (1979).
Nienhuis, A. W., Immer, P. & Bens, E. J. Proc. natn. Acad. Sci. U.S.A. 79, 3960–3964 (1977).
Berk, A. J. & Sharp, P. A. Cell 12, 721–732 (1977).
Weaver, R. F. & Weissman, C. Nucleic Acids Res. 7, 1175–1193 (1979).
Zuniga et al. Cell 34, 535–534 (1983).
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Murre, C., Reiss, C., Bernabeu, C. et al. Construction, expression and recognition of an H—2 molecule lacking its carboxyl terminus. Nature 307, 432–436 (1984). https://doi.org/10.1038/307432a0
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DOI: https://doi.org/10.1038/307432a0
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