Mechanisms of MHC class I-restricted antigen processing and cross-presentation

Immunological Reviews

Volumn 207, Issue , 2005, Pages 145-157

  Cresswell, Peter ^a   Ackerman, Anne L ^a   Giodini, Alessandra ^a   Peaper, David R ^a   Wearsch, Pamela A ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 MICROGLOBULIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEIN P57; TAPASIN;

ANTIGEN PRESENTATION; ANTIGEN PRESENTING CELL; CROSS PRESENTATION; DENDRITIC CELL; DIMERIZATION; DISULFIDE BOND; ENDOCYTOSIS; ENDOPLASMIC RETICULUM; HUMAN; PHAGOSOME; PINOCYTOSIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN LOCALIZATION; PROTEIN SYNTHESIS; REVIEW; T LYMPHOCYTE;

ANIMALS; ANTIGEN PRESENTATION; CROSS-PRIMING; ENDOPLASMIC RETICULUM; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; MODELS, IMMUNOLOGICAL; PEPTIDES;

EID: 26244455510     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0105-2896.2005.00316.x     Document Type: Review

References (62)

1. Wright CA, Kozik P, Zacharias M, Springer S. Tapasin and other chaperones: models of the MHC class I loading complex. Biol Chem 2004;385:763-768.
2. Serwold T, Gonzalez F, Kim J, Jacob R, Shastri N. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 2002;419:480-483.
3. Saric T, et al. An IFN-gamma-induced aminopeptidase in the ER, ERAP1 trims precursors to MHC class I-presented peptides. Nat Immunol 2002;3:1169-1176.
4. York IA, et al. The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nat Immunol 2002;3:1177-1184.
5. Bangia N, Lehner PJ, Hughes EA, Surman M, Cresswell P. The N-terminal region of tapasin is required to stabilize the MHC class I loading complex. Eur J Immunol 1999;29:1858-1870.
6. Momburg F, Tan P. Tapasin-the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum. Mol Immunol 2002;39:217-233.
7. Garbi N, Tiwari N, Momburg F, Hammerling GJ. A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression. Eur J Immunol 2003;33:264-273.
8. Ortmann B, et al. A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes. Science 1997;277:1306-1309.
9. Androlewicz MJ, Ortmann B, van Endert PM, Spies T, Cresswell P. Characteristics of peptide and major histocompatibility complex class I/beta 2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2). Proc Natl Acad Sci USA 1994;91:12716-12720.
10. Suh WK, Cohen-Doyle MF, Fruh K, Wang K, Peterson PA, Williams DB. Interaction of MHC class I molecules with the transporter antigen processing. Science 1994;264:1322-1326.
11. Powis SJ. Major histocompatibility complex class I molecules interact with both subunits of the transporter associated with antigen processing, TAP1 and TAP2. Eur J Immunol 1997;27:2744-2747.
12. Peace-Brewer AL, Tussey LG, Matsui M, Li G, Quinn DG, Frelinger JA. A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL. Immunity 1996;4:505-514.
13. Lewis JW, Neisig A, Neefjes J, Elliott T. Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP. Curr Biol 1996;6:873-883.
14. Harris MR, Yu YY, Kindle CS, Hansen TH, Solheim JC. Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I. J Immunol 1998;160:5404-5409.
15. Kulig K, Nandi D, Bacik I, Monaco JJ, Vukmanovic S. Physical and functional association of the major histocompatibility complex class I heavy chain alpha3 domain with the transporter associated with antigen processing. J Exp Med 1998;187:865-874.
16. Suh WK, et al. Interaction of murine MHC class I molecules with tapasin and TAP enhances peptide loading and involves the heavy chain alpha3 domain. J Immunol 1999;162:1530-1540.
17. Helenius A, Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 2004;73:1019-1049.
18. Wearsch PA, Jakob CA, Vallin A, Dwek RA, Rudd PM, Cresswell P. Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status. J Biol Chem 2004;279:25112-25121.
19. Leach MR, Cohen-Doyle MF, Thomas DY, Williams DB. Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin. J Biol Chem 2002;277:29686-29697.
20. Frickel E-M, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc Natl Acad Sci USA 2002;99:1954-1959.
21. Pollock S, et al. Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system. EMBO J 2004;23:1020-1029.
22. Dick TP, Bangia N, Peaper DR, Cresswell P. Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity 2002;16:87-98.
23. Hughes EA, Hammond C, Cresswell P. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc Natl Acad Sci USA 1997;94:1896-1901.
24. Turnquist HR, et al. The Ig-like domain of tapasin influences intermolecular interactions. J Immunol 2004;172:2976-2984.
25. Patil AR, Thomas CJ, Surolia A. Kinetics and the mechanism of interaction of the endoplasmic reticulum chaperone, calreticulin, with monoglucosylated (Glc1Man9GlcNAc2) substrate. J Biol Chem 2000;275:24348-24356.
26. Sadasivan B, Lehner PJ, Ortmann B, Spies T, Cresswell P. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 1996;5:103-114.
27. Radcliffe CM, Diedrich G, Harvey DJ, Dwek RA, Cresswell P, Rudd PM. Identification of specific glycoforms of major histocompatibility complex class I heavy chains suggests that class I peptide loading is an adaptation of the quality control pathway involving calreticulin and ERp57. J Biol Chem 2002;277:46415-46423.
28. Ahner A, Brodsky JL. Checkpoints in ER-associated degradation: excuse me, which way to the proteasome? Trends Cell Biol 2004;14:474-478.
29. Knittler MR, Alberts P, Deverson EV, Howard JC. Nucleotide binding by TAP mediates association with peptide and release of assembled MHC class I molecules. Curr Biol 1999;9:999-1008.
30. Watts C. Capture and processing of exogenous antigens for presentation on MHC molecules. Annu Rev Immunol 1997;15:821-850.
31. Watts C, Amigorena S. Phagocytosis and antigen presentation. Semin Immunol 2001;13:373-379.
32. Mellman I, Steinman RM. Dendritic cells: specialized and regulated antigen processing machines. Cell 2001;106:255-258.
33. + T cell responses to infectious agents, tumors, transplants, and vaccines. Adv Immunol 1999;73:1-77.
34. Garin J, et al. The phagosome proteasome: insight into phagosome functions. J Cell Biol 2001;152:165-180.
35. Gagnon E, et al. Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages. Cell 2002;110:119-131.
36. Muller-Taubenberger A, Lupas AN, Li H, Ecke M, Simmeth E, Gerisch G. Calreticulin and calnexin in the endoplasmic reticulum are important for phagocytosis. EMBO J 2001;20:6772-6782.
37. Wiertz EJ, et al. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 1996;384:432-438.
38. Rehm A, et al. Human cytomegalovirus gene products US2 and US11 differ in their ability to attack major histocompatibility class I heavy chains in dendritic cells. J Virol 2002;76:5043-5050.
39. Stirling CJ, Rothblatt J, Hosobuchi M, Deshaies R, Schekman R. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol Biol Cell 1992;3:129-142.
40. Wilkinson BM, Tyson JR, Reid PJ, Stirling CJ. Distinct domains within yeast Sec61p involved in post-translational translocation and protein dislocation. J Biol Chem 2000;275:521-529.
41. Lilley BN, Ploegh HL. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 2004;429:834-840.
42. Ye Y, Shibata Y, Yun C, Ron D, Rapoport TA. A membrane protein complex mediates retrotranslocation from the ER lumen into the cytosol. Nature 2004;429:841-847.
43. Knop M, Finger A, Braun T, Hellmuth K, Wolf DH. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J 1996;15:753-763.
44. Guermonprez P, Saveanu L, Kleijmeer M, Davoust J, Van Endert P, Amigorena S. ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells. Nature 2003;425:397-402.
45. Houde M, et al. Phagosomes are competent organelles for antigen cross-presentation. Nature 2003;425:402-406.
46. Rodriguez A, Regnault A, Kleijmeer M, Ricciardi-Castagnoli P, Amigorena S. Selective transport of internalized antigens to the cytosol for MHC class I presentation in dendritic cells. Nat Cell Biol 1999;1:362-368.
47. Ackerman AL, Kyritsis C, Tampe R, Cresswell P. Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens. Proc Natl Acad Sci USA 2003;100:12889-12894.
48. Ackerman AL, Cresswell P. Cellular mechanisms governing cross-presentation of exogenous antigens. Nat Immunol 2004;5:678-684.
49. Norbury CC, Chambers BJ, Prescott AR, Ljunggren HG, Watts C. Constitutive macropinocytosis allows TAP-dependent major histocompatibility complex class I presentation of exogenous soluble antigen by bone marrow-derived dendritic cells. Eur J Immunol 1997;27:280-288.
50. Hengel H, et al. A viral ER-resident glycoprotein inactivates the MHC-encoded peptide transporter. Immunity 1997;6:623-632.
51. Ahn K, et al. The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide translocation by TAP. Immunity 1997;6:613-621.
52. Lehner PJ, Karttunen JT, Wilkinson GW, Cresswell P. The human cytomegalovirus US6 glycoprotein inhibits transporter associated with antigen processing-dependent peptide translocation. Proc Natl Acad Sci USA 1997;94:6904-6909.
53. Kyritsis C, Gorbulev S, Hutschenreiter S, Pawlitschko K, Abele R, Tampe R. Molecular mechanism and structural aspects of transporter associated with antigen processing inhibition by the cytomegalovirus protein US6. J Biol Chem 2001;276:48031-48039.
54. Ackerman AL, Cresswell P. Regulation of MHC class I transport in human dendritic cells and the dendritic-like cell line KG-1. J Immunol 2003;170:4178-4188.
55. Ackerman AL, Kyritsis C, Tampe R, Cresswell P. Access of soluble antigens to the endoplasmic reticulum can explain cross-presentation by dendritic cells. Nat Immunol 2005;6:107-113.
56. Delamarre L, Pack M, Chang H, Mellman I, Trombetta ES. Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate. Science 2005;307:1630-1634.
57. Pelkmans L, Kartenbeck J, Helenius A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat Cell Biol 2001;3:473-483.
58. Lord JM, Roberts LM. Toxin entry: retrograde transport through the secretory pathway. J Cell Biol 1998;140:733-736.
59. Wesche J, Rapak A, Olsnes S. Dependence of ricin toxicity on translocation of the toxin A-chain from the endoplasmic reticulum to the cytosol. J Biol Chem 1999;274:34443-34449.
60. Imai J, Hasegawa H, Maruya M, Koyasu S, Yahara I. Exogenous antigens are processed through the endoplasmic reticulum-associated degradation (ERAD) in cross-presentation by dendritic cells. Int Immunol 2005;17:45-53.
61. Yewdell JW, Anton LC, Bennink JR. Defective ribosomal products (DRiPs): a major source of antigenic peptides for MHC class I molecules? J Immunol 1996;157:1823-1826.
62. Schwab SR, Li KC, Kang C, Shastri N. Constitutive display of cryptic translation products by MHC class I molecules. Science 2003;301:1367-1371.