Immunogenicity of Calreticulin-Bound Murine Leukemia Virus Glycoprotein gp90

  • Yusuke Mimura
  • Denise Golgher
  • Yuka Mimura-Kimura
  • Raymond A. Dwek
  • Pauline M. Rudd
  • Tim Elliott
Conference paper
Part of the Advances in Experimental Medicine and Biology book series (AEMB)

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Adorini, L., Appella, E., Doria, G., Cardinaux, F. and Nagy, Z.A. (1989) Competition for antigen presentation in living cells involves exchange of peptides bound by class II MHC molecules. Nature, 342, 800–803.CrossRefPubMedGoogle Scholar
  2. Allen, P.M. and Unanue, E.R. (1984) Differential requirements for antigen processing by macrophages for lysozyme-specific T cell hybridomas. J Immunol, 132, 1077–1079.PubMedGoogle Scholar
  3. Castellino, F., Zappacosta, F., Coligan, J.E. and Germain, R.N. (1998) Large protein fragments as substrates for endocytic antigen capture by MHC class II molecules. J Immunol, 161, 4048–4057.PubMedGoogle Scholar
  4. Chesnut, R.W., Endres, R.O. and Grey, H.M. (1980) Antigen recognition by T cells and B cells: recognition of cross-reactivity between native and denatured forms of globular antigens. Clin Immunol Immunopathol, 15, 397–408.CrossRefPubMedGoogle Scholar
  5. Cresswell, P. (1994) Assembly, transport, and function of MHC class II molecules. Annu Rev Immunol, 12, 259–293.CrossRefPubMedGoogle Scholar
  6. Deng, H., Apple, R., Clare-Salzler, M., Trembleau, S., Mathis, D., Adorini, L. and Sercarz, E. (1993) Determinant capture as a possible mechanism of protection afforded by major histocompatibility complex class II molecules in autoimmune disease. J Exp Med, 178, 1675–1680.CrossRefPubMedGoogle Scholar
  7. Denzin, L.K. and Cresswell, P. (1995) HLA-DM induces CLIP dissociation from MHC class II alpha beta dimers and facilitates peptide loading. Cell, 82, 155–165.CrossRefPubMedGoogle Scholar
  8. Donermeyer, D.L. and Allen, P.M. (1989) Binding to Ia protects an immunogenic peptide from proteolytic degradation. J Immunol, 142, 1063–1068.PubMedGoogle Scholar
  9. Fass, D., Davey, R.A., Hamson, C.A., Kim, P.S., Cunningham, J.M. and Berger, J.M. (1997) Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution. Science, 277, 1662–1666.CrossRefPubMedGoogle Scholar
  10. Germain, R.N. (1994) MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell, 76, 287–299.CrossRefPubMedGoogle Scholar
  11. Gliniak, B.C., Kozak, S.L., Jones, R.T. and Kabat, D. (1991) Disulfide bonding controls the processing of retroviral envelope glycoproteins. J Biol Chem, 266, 22991–22997.PubMedGoogle Scholar
  12. Golgher, D., Korangy, F., Gao, B., Gorski, K., Jaffee, E., Edidin, M., Pardoll, D.M. and Elliott, T. (2001) An immunodominant MHC class II-restricted tumor antigen is conformation dependent and binds to the endoplasmic reticulum chaperone, calreticulin. J Immunol, 167, 147–155.CrossRefPubMedGoogle Scholar
  13. Griffin, J.P., Chu, R. and Harding, C.V. (1997) Early endosomes and a late endocytic compartment generate different peptide-class II MHC complexes via distinct processing mechanisms. J Immunol, 158, 1523–1532.PubMedGoogle Scholar
  14. Harding, C.V. and Unanue, E.R. (1989) Antigen processing and intracellular Ia. Possible roles of endocytosis and protein synthesis in Ia function. J Immunol, 142, 12–19.PubMedGoogle Scholar
  15. Helenius, A. and Aebi, M. (2001) Intracellular functions of N-linked glycans. Science, 291, 2364–2369.CrossRefPubMedGoogle Scholar
  16. Hiltbold, E.M. and Roche, P.A. (2002) Trafficking of MHC class II molecules in the late secretory pathway. Curr Opin Immunol, 14, 30–35.CrossRefPubMedGoogle Scholar
  17. Housseau, F., Moorthy, A., Langer, D.A., Robbins, P.F., Gonzales, M.I. and Topalian, S.L. (2001) N-linked carbohydrates in tyrosinase are required for its recognition by human MHC class II-restricted CD4(+) T cells. Eur J Immunol, 31, 2690–2701.CrossRefPubMedGoogle Scholar
  18. Huang, A.Y., Gulden, P.H., Woods, A.S., Thomas, M.C., Tong, C.D., Wang, W., Engelhard, V.H., Pasternack, G., Cotter, R., Hunt, D., Pardoll, D.M. and Jaffee, E.M. (1996) The immunodominant major histocompatibility complex class I-restricted antigen of a murine colon tumor derives from an endogenous retroviral gene product. Proc Natl Acad Sci USA, 93, 9730–9735.CrossRefPubMedPubMedCentralGoogle Scholar
  19. Jensen, P.E. (1993) Acidification and disulfide reduction can be sufficient to allow intact proteins to bind class II MHC. J Immunol, 150, 3347–3356.PubMedGoogle Scholar
  20. Lee, P., Matsueda, G.R. and Allen, P.M. (1988) T cell recognition of fibrinogen. A determinant on the A alpha-chain does not require processing. J Immunol, 140, 1063–1068.PubMedGoogle Scholar
  21. Lenz, J., Crowther, R., Straceski, A. and Haseltine, W. (1982) Nucleotide sequence of the Akv env gene. J Virol, 42, 519–529.PubMedPubMedCentralGoogle Scholar
  22. Lindner, R. and Unanue, E.R. (1996) Distinct antigen MHC class II complexes generated by separate processing pathways. Embo J, 15, 6910–6920.PubMedPubMedCentralGoogle Scholar
  23. Ma, C., Whiteley, P.E., Cameron, P.M., Freed, D.C., Pressey, A., Chen, S.L., Garni-Wagner, B., Fang, C., Zaller, D.M., Wicker, L.S. and Blum, J.S. (1999) Role of APC in the selection of immunodominant T cell epitopes. J Immunol, 163, 6413–6423.PubMedGoogle Scholar
  24. Nadimi, F., Moreno, J., Momburg, F., Heuser, A., Fuchs, S., Adorini, L. and Hammerling, G.J. (1991) Antigen presentation of hen egg-white lysozyme but not of ribonuclease A is augmented by the major histocompatibility complex class II-associated invariant chain. Eur J Immunol, 21, 1255–1263.CrossRefPubMedGoogle Scholar
  25. Nelson, C.A., Roof, R.W., McCourt, D.W. and Unanue, E.R. (1992) Identification of the naturally processed form of hen egg white lysozyme bound to the murine major histocompatibility complex class II molecule I-Ak. Proc Natl Acad Sci USA, 89, 7380–7383.CrossRefPubMedPubMedCentralGoogle Scholar
  26. Pardoll, D.M. and Topalian, S.L. (1998) The role of CD4+ T cell responses in antitumor immunity. Curr Opin Immunol, 10, 588–594.CrossRefPubMedGoogle Scholar
  27. Parodi, A.J. (2000) Protein glucosylation and its role in protein folding. Annu Rev Biochem, 69, 69–93.CrossRefPubMedGoogle Scholar
  28. Pinet, V., Malnati, M.S. and Long, E.O. (1994) Two processing pathways for the MHC class II-restricted presentation of exogenous influenza virus antigen. J Immunol, 152, 4852–4860.PubMedGoogle Scholar
  29. Pinet, V., Vergelli, M., Martin, R., Bakke, O. and Long, E.O. (1995) Antigen presentation mediated by recycling of surface HLA-DR molecules. Nature, 375, 603–606.CrossRefPubMedGoogle Scholar
  30. Pinter, A. and Fleissner, E. (1977) The presence of disulfide-linked gp70-p15(E) complexes in AKR murine leukemia virus. Virology, 83, 417–422.CrossRefPubMedGoogle Scholar
  31. Pinter, A., Lieman-Hurwitz, J. and Fleissner, E. (1978) The nature of the association between the murine leukemia virus envelope proteins. Virology, 91, 345–351.CrossRefPubMedGoogle Scholar
  32. Sercarz, E.E., Lehmann, P.V., Ametani, A., Benichou, G., Miller, A. and Moudgil, K. (1993) Dominance and crypticity of T cell antigenic determinants. Annu Rev Immunol, 11, 729–766.CrossRefPubMedGoogle Scholar
  33. Sercarz, E.E. and Maverakis, E. (2003) Mhc-guided processing: binding of large antigen fragments. Nat Rev Immunol, 3, 621–629.CrossRefPubMedGoogle Scholar
  34. Sette, A., Adorini, L., Colon, S.M., Buus, S. and Grey, H.M. (1989) Capacity of intact proteins to bind to MHC class II molecules. J Immunol, 143, 1265–1267.PubMedGoogle Scholar
  35. Sherman, M.A., Weber, D.A. and Jensen, P.E. (1995) DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide. Immunity, 3, 197–205.CrossRefPubMedGoogle Scholar
  36. Sitia, R. and Braakman, I. (2003) Quality control in the endoplasmic reticulum protein factory. Nature, 426, 891–894.CrossRefPubMedGoogle Scholar
  37. Sjolander, S., Bolmstedt, A., Akerblom, L., Horal, P., Olofsson, S., Morein, B. and Sjolander, A. (1996) N-linked glycans in the CD4-binding domain of human immunodeficiency virus type 1 envelope glycoprotein gp160 are essential for the in vivo priming of T cells recognizing an epitope located in their vicinity. Virology, 215, 124–133.CrossRefPubMedGoogle Scholar
  38. Sloan, V.S., Cameron, P., Porter, G., Gammon, M., Amaya, M., Mellins, E. and Zaller, D.M. (1995) Mediation by HLA-DM of dissociation of peptides from HLA-DR. Nature, 375, 802–806.CrossRefPubMedGoogle Scholar
  39. Streicher, H.Z., Berkower, I.J., Busch, M., Gurd, F.R. and Berzofsky, J.A. (1984) Antigen conformation determines processing requirements for T-cell activation. Proc Natl Acad Sci USA, 81, 6831–6835.CrossRefPubMedPubMedCentralGoogle Scholar
  40. Surman, S., Lockey, T.D., Slobod, K.S., Jones, B., Riberdy, J.M., White, S.W., Doherty, P.C. and Hurwitz, J.L. (2001) Localization of CD4+ T cell epitope hotspots to exposed strands of HIV envelope glycoprotein suggests structural influences on antigen processing. Proc Natl Acad Sci USA, 98, 4587–4592.CrossRefPubMedPubMedCentralGoogle Scholar
  41. Trombetta, E.S. (2003) The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis. Glycobiology, 13, 77R–91R.CrossRefPubMedGoogle Scholar
  42. Villadangos, J.A., Driessen, C., Shi, G.P., Chapman, H.A. and Ploegh, H.L. (2000) Early endosomal maturation of MHC class II molecules independently of cysteine proteases and H-2DM. Embo J, 19, 882–891.CrossRefPubMedPubMedCentralGoogle Scholar
  43. Viner, N.J., Nelson, C.A. and Unanue, E.R. (1995) Identification of a major I-Ek-restricted determinant of hen egg lysozyme: limitations of lymph node proliferation studies in defining immunodominance and crypticity. Proc Natl Acad Sci USA, 92, 2214–2218.CrossRefPubMedPubMedCentralGoogle Scholar
  44. Watts, C. (2001) Antigen processing in the endocytic compartment. Curr Opin Immunol, 13, 26–31.CrossRefPubMedGoogle Scholar
  45. Watts, C. (2004) The exogenous pathway for antigen presentation on major histocompatibility complex class II and CD1 molecules. Nat Immunol, 5, 685–692.CrossRefPubMedGoogle Scholar
  46. Wolf, P.R. and Ploegh, H.L. (1995) How MHC class II molecules acquire peptide cargo: biosynthesis and trafficking through the endocytic pathway. Annu Rev Cell Dev Biol, 11, 267–306.CrossRefPubMedGoogle Scholar
  47. Zhong, G., Romagnoli, P. and Germain, R. N. (1997) Related leucine-based cytoplasmic targeting signals in invariant chain and major histocompatibility complex class II molecules control endocytic presentation of distinct determinants in a single protein. J Exp Med, 185, 429–438.CrossRefPubMedPubMedCentralGoogle Scholar

Copyright information

© Springer 2005

Authors and Affiliations

  • Yusuke Mimura
    • 1
    • 2
  • Denise Golgher
    • 2
  • Yuka Mimura-Kimura
    • 1
  • Raymond A. Dwek
    • 1
  • Pauline M. Rudd
    • 1
  • Tim Elliott
    • 2
  1. 1.Glycobiology Institute Department of BiochemistryUniversity of OxfordOxfordUK
  2. 2.Cancer Sciences Division School of MedicineUniversity of SouthamptonSouthamptonUK

Personalised recommendations