Analysis of the early biogenesis of CD1b: Involvement of the chaperones calnexin and calreticulin, the proteasome and β2-microglobulin

International Immunology

Volumn 11, Issue 10, 1999, Pages 1615-1623

  Hüttinger, Robert ^a   Staffler, Günther ^a   Majdic, Otto ^a   Stockinger, Hannes ^a  

^a UNIVERSITY OF VIENNA   (Austria)

Author keywords

Antigen presentation; CD1; Chaperones; MHC

Indexed keywords

BETA 2 MICROGLOBULIN; CALNEXIN; CALRETICULIN; CASTANOSPERMINE; CD1 ANTIGEN; CHAPERONE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MANNOSIDASE; PROTEASOME; PROTEIN;

ANTIGEN BINDING; ARTICLE; BIOGENESIS; CELL LINE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENDOSOME; HUMAN; HUMAN CELL; MELANOMA CELL; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN SYNTHESIS;

ANTIGENS, CD; ANTIGENS, CD1; BETA 2-MICROGLOBULIN; BETA-GLUCOSIDASE; CALCIUM-BINDING PROTEINS; CALNEXIN; CALRETICULIN; CELL LINE; CYSTEINE ENDOPEPTIDASES; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; INDOLIZINES; MANNOSIDASES; MOLECULAR CHAPERONES; MONOCYTES; MULTIENZYME COMPLEXES; PROTEASOME ENDOPEPTIDASE COMPLEX; RIBONUCLEOPROTEINS; TRANSFECTION;

EID: 0345425612     PISSN: 09538178     EISSN: None     Source Type: Journal    
DOI: 10.1093/intimm/11.10.1615     Document Type: Article

References (49)

1. Zeng, Z. H., Castano, A. R., Segelke, B. W., Stura, E. A., Peterson, P. A. and Wilson, I. A. 1997. Crystal structure of mouse CD1: an MHC-like fold with a large hydrophobic binding groove. Science 277:339.
2. + T cells. Nature 372:691.
3. Sieling, P. A., Chatterjee, D., Porcelli, S. A., Prigozy, T. I., Mazzaccaro, R. J., Soriano, T., Bloom, B. R., Brenner, M. B., Kronenberg, M., Brennan, P. J. and Modlin, R. L. 1995. CD1-restricted T cell recognition of microbial lipoglycan antigens. Science 269:227.
4. Jackman, R. M., Stenger, S., Lee, A., Moody, D. B., Rogers, R. A., Niazi, K. R., Sugita, M., Modlin, R. L., Peters, P. J. and Porcelli, S. A. 1998. The tyrosine-containing cytoplasmic tail of CD1b is essential for its efficient presentation of bacterial lipid antigens. Immunity 8:341.
5. Prigozy, T. I., Sieling, P. A., Clemens, D., Stewart, P. L., Behar, S. M., Porcelli, S. A., Brenner, M. B., Modlin, R. L. and Kronenberg, M. 1997. The mannose receptor delivers lipoglycan antigens to endosomes for presentation to T cells by CD1b molecules. Immunity 6:187.
6. Sugita, M., Jackman, R. M., van Donselaar, E., Behar, S. M., Rogers, R. A., Peters, P. J., Brenner, M. B. and Porcelli, S. A. 1996. Cytoplasmic tail-dependent localization of CD1b antigen-presenting molecules to MIICs. Science 273:349.
7. Ernst, W. A., Maher, J., Cho, S., Niazi, K. R., Chatterjee, D., Moody, D. B., Besra, G. S., Watanabe, Y., Jensen, P. E., Porcelli, S. A., Kronenberg, M. and Modlin, R. L. 1998. Molecular interaction of CD1b with lipoglycan antigens. Immunity 8:331.
8. 2-microglobulin for expression and formation of human CD1 antigens. Eur J. Immunol. 27:1366.
9. 2-microglobulin-dependent surface expression of functional mouse CD1.1. J. Exp. Med. 182:1913.
10. Sugita, M., Porcelli, S. A. and Brenner, M. B. 1997. Assembly and retention of CD1b heavy chains in the endoplasmic reticulum. J. Immunol. 159:2358.
11. Rajagopalan, S. and Brenner, M. B. 1994. Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum. J. Exp. Med. 180:407.
12. Vassilakos, A., Cohen-Doyle, M. F., Peterson, P. A., Jackson, M. R. and Williams, D. B. 1996. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J. 15:1495.
13. Hammond, C., Braakman, I. and Helenius, A. 1994. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl Acad. Sci. USA 91:913.
14. Hubbard, S. C. and Ivatt, R. J. 1981. Synthesis and processing of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 50:555.
15. 2 oligosaccharide as an initial step in recognizing unfolded glyccproteins. J. Biol. Chem. 270:4697.
16. Moore, S. E. and Spiro, R. G. 1993. Inhibition of glucose trimming by castanospermine results in rapid degradation of unassembled major histocompatibility complex class I molecules. J. Biol. Chem. 268:3809.
17. 2-microglobulin, class I heavy chain conformation, and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing. J. Immunol. 158:2236.
18. Peterson, J. R., Ora, A., Van, P. N. and Helenius, A. 1995. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol. Biol. Cell 6:1173.
19. Hebert, D. N., Zhang, J. X., Chen, W., Foellmer, B. and Helenius, A. 1997. The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. J. Cell Biol. 139:613.
20. van Leeuwen, J. E. and Kearse, K. P. 1996. The related molecular chaperones calnexin and calreticulin differentially associate with nascent T cell antigen receptor proteins within the endoplasmic reticulum. J. Biol. Chem. 271:25345.
21. Zhang, Q. and Salter, R. D. 1998. Distinct patterns of folding and interactions with calnexin and calreticulin in human class I MHC proteins with altered N-glycosylation. J. Immunol. 160:831.
22. Wei, M. L. and Cresswell, P. 1992. HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. Nature 356:443.
23. Peters, P. J., Neefjes, J. J., Oorschot, V., Ploegh, H. L. and Geuze, H. J. 1991. Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments. Nature 349:669.
24. Hughes, E. A., Hammond, C. and Cresswell, P. 1997. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc. Natl Acad. Sci. USA 94:1896.
25. Baier, G., Baier-Bitterlich, G., Couture, C., Telford, D., Giampa, L. and Altman, A. 1994. An efficient expression, purification and immunodetection system for recombinant gene products. Biotechniques 17:94.
26. Olive, D., Dubreuil, P. and Mawas, C. 1984. Two distinct TL-like molecular subsets defined by monoclonal antibodies on the surface of human thymocytes with different expression on leukemia lines. Immunogenetics 20:253.
27. Stam, N. J., Spits, H. and Ploegh, H. L. 1986. Monoclonal antibodies raised against denatured HLA-B locus heavy chains permit biochemical characterization of certain HLA-C locus products. J. Immunol. 137:2299.
28. Barnstable, C. J., Bodmer, W. F., Brown, G., Galfre, G., Milstein, C., Williams, A. F. and Ziegler, A. 1978. Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens - new tools for genetic analysis. Cell 14:9.
29. 2-microglobulin antibody and its use in the genetic and biochemical analysis of major histocompatibility antigens. Eur. J. Immunol. 9:536.
30. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
31. Kasinrerk, W., Fiebiger, E., Stefanova, I., Baumruker, T., Knapp, W. and Stockinger, H. 1992. Human leukocyte activation antigen M6, a member of the Ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule. J. Immunol. 149:847.
32. Sadasivan, B., Lehner, P. J., Ortmann, B., Spies, T. and Cresswell, P. 1996. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5:103.
33. Hebert, D. N., Foellmer, B. and Helenius, A. 1995. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81:425.
34. Balow, J. P., Weissman, J. D. and Kearse, K. P. 1995. Unique expression of major histocompatibility complex class I proteins in the absence of glucose trimming and calnexin association. J. Biol. Chem. 270:29025.
35. McCracken, A. A. and Brodsky, J. L. 1996. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J. Cell Biol. 132:291.
36. Fenteany, G., Standaert, R. F., Lane, W. S., Choi, S., Corey, E. J. and Schreiber, S. L. 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:726.
37. Yang, M., Omura, S., Bonifacino, J. S. and Weissman, A. M. 1998. Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes. J. Exp. Med. 187:835.
38. Kasinrerk, W., Baumruker, T., Majdic, O., Knapp, W. and Stockinger, H. 1993. CD1 molecule expression on human monocytes induced by granulocyte-macrophage colony-stimulating factor. J. Immunol. 150:579.
39. - T lymphocytes to a microbial antigen. Nature 360:593,
40. Porcelli, S. A. 1995. The CD1 family: a third lineage of antigen-presenting molecules. Adv. Immunol. 59:1.
41. Lindquist, J. A., Jensen, O. N., Mann, M. and Hämmerling, G. J. 1998. ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J. 17:2186.
42. 2-Microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteins. Mol. Immunol. 34:401.
43. Ward, C. L., Omura, S. and Kopito, R. R. 1995. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83:121.
44. Jensen, T. J., Loo, M. A., Pind, S., Williams, D. B., Goldberg, A. L. and Riordan, J. R. 1995. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83:129.
45. Wiertz, E. J., Jones, T. R., Sun, L., Bogyo, M., Geuze, H. J. and Ploegh, H. L. 1996. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84:769.
46. Wiertz, E. J., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T. R., Rapoport, T. A. and Ploegh, H. L. 1996. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384:432.
47. 1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J. Biol. Chem. 271:22791.
48. Hochstrasser, M. 1995. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7:215.
49. 1-antitrypsin involves release from calnexin and post-translational trimming of asparagine-linked oligosaccharides. J. Biol. Chem. 272:7946.