Calreticulin displays in vivo peptide-binding activity and can elicit CTL responses against bound peptides

Journal of Immunology

Volumn 162, Issue 11, 1999, Pages 6426-6432

  Nair, Smita ^a   Wearsch, Pamela A ^a   Mitchell, Duane A ^a   Wassenberg, James J ^a   Gilboa, Eli ^a   Nicchitta, Christopher V ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CALRETICULIN; CHAPERONE; LECTIN; PEPTIDE;

ANIMAL CELL; ANTIGENICITY; ARTICLE; CELLULAR IMMUNITY; CONTROLLED STUDY; CYTOTOXIC T LYMPHOCYTE; DENDRITIC CELL; ENDOPLASMIC RETICULUM; FEMALE; MOLECULAR RECOGNITION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; T LYMPHOCYTE SUBPOPULATION;

ANIMALS; ANTIGEN PRESENTATION; CALCIUM-BINDING PROTEINS; CALRETICULIN; CELL LINE; CYTOTOXICITY, IMMUNOLOGIC; DENDRITIC CELLS; EPITOPES, T-LYMPHOCYTE; FEMALE; HSP70 HEAT-SHOCK PROTEINS; MEMBRANE PROTEINS; MICE; MICE, INBRED C57BL; MICE, SCID; MOLECULAR CHAPERONES; OVALBUMIN; PEPTIDES; PROTEIN BINDING; RIBONUCLEOPROTEINS; T-LYMPHOCYTES, CYTOTOXIC; TUMOR CELLS, CULTURED;

EID: 0033152788     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (34)

1. Nash, P. D., M. Opas, and M. Michalak. 1994. Calreticulin: not just another calcium binding protein. Mol. Cell. Biochem. 135:71.
2. Hebert, D. N., B. Foellmer, and A. Helenius. 1996. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J. 15:2961.
3. Vassilakos, A., M. Michalak, M. A. Lehrman, and D. B. Williams. 1998. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 37:3480.
4. Spiro. R. G., Q. Zhu, V. Bhoyroo, and H. Soling. 1996. Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J. Biol. Chem. 271: 11588.
5. Hebert, D. N., J. X. Zhang, W. Chen, B. Foellmer, and A. Helenius. 1997. The number and location of glycans on influenza hernagglutinin determine folding and association with calnexin and calreticulin. J. Cell Biol. 139:613.
6. Sadasivan, B., P. J. Lehner, B. Ortmann, T. Spies, and P. Cressell. 1996. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Cell 5:103.
7. Ortmann, B., J. Copeman, P. J. Lehner, B. Sadasivan, J. A. Herberg, A. G. Grandea, S. R. Riddell, R. Tampe, T. Spies, J. Trowsdale, and P. Cressell. 1997. A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes. Science 277:1306.
8. 2-microglobulin, class I heavy chain conformation, and tapasin in the interactions of class 1 heavy chain with calreticulin and the transporter associated with antigen processing. J. Immunol. 158:2236.
9. Powis, S. J. 1997. Major histocompatability complex class I molecules interact with both subunits of the transporter associated with antigen processing, TAP1 and TAP2. Eur. J. Immunol. 27:2744.
10. Spee, P., and J. Neefjes. 1997. TAP-translocaled peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disultide isomerase and calreticulin. Eur J. Immunol. 27:2441.
11. Blachere, N. E., Z. Li, R. Y. Chandawarkar, R. Suto, N. S. Jaikaria, S. Basu, H. Udono, and P. K. Srivastava. 1997. Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity. J. Exp. Med. 186:1315.
12. Wearsch, P. A., and C. V. Nicchitta. 1997. Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenine nucleotide-independent. J. Biol. Chem. 272:5152.
13. Noiva, R., H. Kimura, J. Roos, and W. J. Lennarz. 1991. Peptide binding by protein disulflde isomerase, a resident protein of the endoplasmic reticulum lumen. J. Biol. Chem. 266:19645.
14. Flynn, G. C., T. G. Chappell, and J. E. Rothman. 1989. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245:385.
15. Lammert, E., S. Stevanovic, H.-G. Rammensee, and H. Schild. 1997. Protein disulflde isomerase is the dominant acceptor for peptides translocated into the endoplasmic reticulum. Eur. J. Immunol. 27:1685.
16. Suto, R., and P. K. Srivastava. 1995. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 269:1585.
17. Arnold, D., S. Faath, H.-G. Rammensee, and H. Schild. 1995. Cross-priming of minor histocompatability antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96. J. Exp. Med. 182:885.
18. Nicchitta, C. V. 1998. Biochemical, cell biological, and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96. Curr. Opin. Immunol. 10:103.
19. Tamura, Y., P. Peng, K. Liu, M. Daou, and P. K. Srivastava. 1997. Immunotherapy of cancers with autologous cancer-derived heat shock protein preparations. Science 278:117.
20. + cytotoxic T lymphocytes. Proc. Natl. Acad. Sci. USA 87:9015.
21. Wearsch, P. A., and C. V. Nicchitta. 1996. Purification and partial molecular characterization of GRP94, an ER resident chaperone. Protein Expr. Purif. 7:114.
22. Tack, B. F., J. Dean, D. Eilat, P. E. Lorenr, and A. N. Schechter. 1980. Tritium labeling of proteins to high specific radioactivity by reductive methylation. J. Biol. Chem. 255:8842.
23. Mitchell, D. A., S. K. Nair, and E. Gilboa. 1998. Dendritic cell/macrophage precursors capture exogenous antigen for MHC class I presentation by dendritic cells. Eur. J. Immunol. 28:1923.
24. Nair, S. K., D. Snyder, B. T. Rouse, and E. Gilboa. 1997. Regression of tumors in mice vaccinated with professional antigen-presenting cells pulsed with tumor extracts. Int. J. Cancer 70:706.
25. Boczkowski, D., S. K. Nair, D. Snyder, and E. Gilboa. 1996. Dendritic cells pulsed with RNA are potent antigen-presenting cells in vitro and in vivo. J. Exp. Med. 184:465.
26. Porgador, A., Feldman, M., and Eisenbach, L. 1989. H-2Kb transfection of B16 melanoma cells results in reduced tumorigenicity and metastatic competence. J. Immunogenet. 16:291.
27. Moore, M. W., Carbone, F. R., and Bevan, M. J. 1988. Introduction of soluble protein into class I pathway of antigen processing and presentation. Cell 54:777.
28. Steinman, R. M. 1991. The dendritic cell system and its role in immunogenicity. Annu. Rev. Immunol. 9:271.
29. Matzinger, P. 1994. Tolerance, danger and the extended family. Annu. Rev. Immunol. 12:991.
30. Carbone, F. R., C. Kurts, S. R. M. Bennett, J. F. A. P. Miller, and W. R. Heath. 1998. Cross-presentation: a general mechanism for CTL immunity and tolerance. Immunol. Today 19:103.
31. Srivastava, P. K., A. Menoret, S. Basu, R. J. Binder, and K. L. McQuade. 1998. Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world. Immunity 8:657.
32. Fearon, E. R., T. Itaya, B. Hunt, B. Vogelstein, and P. Frost. 1988. Induction in a murine tumor of immunogenic tumor variants by transfection with a foreign gene. Cancer Res. 48:2975.
33. Watts, C. 1997. Capture and processing of exogenous antigens for presentation on MHC molecules. Annu. Rev. Immunol. 15:821.
34. Bevan, M. J. 1995. Antigen presentation to cytotoxic T lymphocytes in vivo. J. Exp. Med. 182:639.