Presentation of antigenic peptides by products of the major histocompatibility complex

Journal of Peptide Science

Volumn 4, Issue 3, 1998, Pages 182-194

  Fairchild, Paul J ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Anchor residues; Hydrophobic pockets; MHC class I; MHC class II; Peptide binding groove; Peptide termini

Indexed keywords

EPITOPE; HLA ANTIGEN CLASS 1; HLA ANTIGEN CLASS 2; LYMPHOCYTE ANTIGEN RECEPTOR; PEPTIDE;

ANIMAL; CHEMISTRY; HUMAN; IMMUNOLOGY; MAJOR HISTOCOMPATIBILITY COMPLEX; REVIEW;

ANIMALS; EPITOPES; HISTOCOMPATIBILITY ANTIGENS CLASS I; HISTOCOMPATIBILITY ANTIGENS CLASS II; HUMANS; MAJOR HISTOCOMPATIBILITY COMPLEX; PEPTIDES; RECEPTORS, ANTIGEN, T-CELL;

EID: 0032059367     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1099-1387(199805)4:3<182::aid-psc144>3.0.co;2-s     Document Type: Review

References (82)

1. J.K. Pullen, R.M. Horton, Z. Cai and L.R. Pease (1992). Structural diversity of the classical H-2 genes: K, D, and L. J. Immunol. 148, 953-967.
2. P.J. Bjorkman, M. Saper, B. Samraoui, W.S. Bennett, J.L. Strominger and D.C. Wiley (1987). Structure of the human class I histocompatibility antigen, HLA-A2. Nature 329, 506-512.
3. T.P.J. Garrett, M.A. Saper, P.J. Bjorkman, J.L. Strominger and D.C. Wiley (1989). Specificity pockets for the side chains of peptide antigens in HLA-Aw68. Nature 342, 692-696.
4. J.H. Brown, T.S. Jardetzky, J.C. Gorga, L.J. Stern, R.G. Urban, J.L. Strominger and D.C. Wiley (1993). Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature 364, 33-39.
5. S. Weber, A. Traunecker, F. Oliveri, W. Gerhard and K. Karjalainen (1992). Specific low-affinity recognition of major histocompatibility complex plus peptide by soluble T-cell receptor. Nature 356, 793-796.
6. K. Matsui, J.J. Boniface, P.A. Reay, H. Schild, B. Fazekas de St Groth and M.M. Davis (1991). Low affinity interaction of peptide-MHC complexes with T cell receptors. Science 254, 1788-1791.
7. D.H. Fremont, W.A. Rees and H. Kozono (1996). Biophysical studies of T-cell receptors and their ligands. Curr. Opin. Immunol. 8, 93-100.
8. T.N.M. Schumacher, L.H. De Bruijn, L.N. Vernie, W.M. Kast, C.J.M. Melief, J.J. Neefjes and H.L. Ploegh (1991). Peptide selection by MHC class I molecules. Nature 350, 703-706.
9. D.R. Madden, J.C. Gorga, J.L. Strominger and D.C. Wiley (1991). The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation. Nature 353, 321-325.
10. M.L. Silver, H.-C. Guo, J.L. Strominger and D.C. Wiley (1992). Atomic structure of a human MHC molecule presenting an influenza virus peptide. Nature 360, 367-369.
11. H.-C. Guo, T.S. Jardetzky, T.P.J. Garrett, W.S. Lane, J.L. Strominger and D.C. Wiley (1992). Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle. Nature 360, 364-366.
12. M. Matsumura, D.H. Fremont, P.A. Peterson and I.A. Wilson (1992). Emerging principles for the recognition of peptide antigens by MHC class I molecules. Science 257, 927-934.
13. F. Latron, L. Pazmany, J. Morrison, R. Motts, M.S. Saper, A. McMichael and J.L. Strominger (1992). A critical role for conserved residues in the cleft of HLA-A2 in presentation of a nonapeptide to T cells. Science 257, 964-967.
14. M. Bouvier and D.C. Wiley (1994). Importance of peptide amino and carboxyl termini to the stability of MHC class I molecules. Science 265, 398-402.
15. K.J. Smith, S.W. Reid, K. Harlos, A.J. McMichael, D.I. Stuart, J.I. Bell and E.Y. Jones (1996). Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. Immunity 4, 215-228.
16. d with beta-2 microglobulin and peptide. Proc. Natl. Acad. Sci. USA 94, 6880-6885.
17. b molecule containing a single viral peptide: Implications for peptide binding and T-cell receptor recognition. Proc. Natl. Acad. Sci. USA 89, 8403-8407.
18. C.-R. Wang, A.R. Castaño, P.A. Peterson, C. Slaughter, K.F. Lindahl and J. Deisenhofer (1995). Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3. Cell. 82, 655-664.
19. E.J. Collins, D.N. Garboczi and D.C. Wiley (1994). Three-dimensional structure of a peptide extending from one end of a class I MHC binding site. Nature 371, 626-629.
20. b. Science 257, 919-927.
21. M. Barinaga (1992). Getting some 'backbone': How MHC binds peptides. Science 257, 880-881.
22. K. Falk, O. Rötzschke and H.-G. Rammensee (1990). Cellular peptide composition governed by major histocompability complex class I molecules. Nature 348, 248-251.
23. T. Elliott, M. Smith, P. Driscoll and A. McMichael (1993). Peptide selection by class I molecules of the major histocompability complex. Curr. Biol. 3, 854-866.
24. V.H. Engelhard (1994). Structure of peptides associated with MHC class I molecules. Curr. Opin. Immunol. 6, 13-23.
25. T.S Jardetzky, W.S. Lane, R.A. Robinson, D.R. Madden and D.C. Wiley (1991). Identification of self peptides bound to purified HLA-B27. Nature 353, 326-329.
26. K. Falk, O. Rötzschke, S. Stevanovic, G. Jung and H.-G. Rammensee (1991). Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 351, 290-296.
27. b molecule. Nature 348, 213-216.
28. C.J. Thorpe (1993). Outsize peptides bulge out of the groove. Immunol. Today 14, 51-52.
29. b at 2.4 Å resolution: Implications for antigen-determinant selection. Cell 76, 39-50.
30. E.Y. Jones (1997). MHC class I and class II structures. Curr. Opin. Immunol. 9, 75-79.
31. b-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove. Proc. Natl Acad. Sci. USA 92, 2479-2483.
32. D.R. Madden, D.N. Garboczi and D.C. Wiley (1993). The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75, 693-708.
33. B.A. Fields, B. Ober, E.L. Malchiodi, M.I. Lebedeva, B.C. Braden, X. Yserm, J.-K. Kim, X. Shao, E.S. Ward and R.A. Mariuzza (1995). Crystal structure of the Vα domain of a T cell antigen receptor. Science 270, 1821-1824.
34. G.A. Bentley, G. Boulot, K. Karjalainen, R.A. Mariuza (1995). Crystal structure of the β chain of a T cell antigen receptor. Science 267, 1984-1987.
35. P. Marrack and J. Kappler (1988). The T-cell repertoire for antigen and MHC. Immunol. Today 9, 308-315.
36. M.M. Davis and Y.-H. Chien (1993). Topology and affinity of T-cell receptor mediated recognition of peptide-MHC complexes. Curr. Opin. Immunol. 5, 45-49.
37. P.J. Bjorkman (1997). MHC restriction in three dimensions: A view of T cell receptor/ligand interactions. Cell 89, 167-170.
38. D.N. Garboczi, P. Ghosh, U. Utz, Q.R. Fan, W.E. Biddison and D.C. Wiley (1996). Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384, 134-141.
39. K.C. Garcia, M. Degano, R.L. Stanfield, A. Brunmark, M.R. Jackson, P.A. Peterson, L. Teyton and I.A. Wilson (1996). An αβ T cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex. Science 274, 209-219.
40. b molecule. Immunity 3, 573-582.
41. B. Catipovic, J. Dal Porto, M. Mage, T.E. Johansen and J.P. Schneck (1992). Major histocompatibility complex conformational epitopes are peptide specific. J. Exp. Med. 176, 1611-1618.
42. J.A. Bluestone, S. Jameson, S. Miller and R. Dick (1992). Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition. J. Exp. Med. 176, 1757-1761.
43. K.J. Smith, S.W. Reid, D.I. Stuart, A.J. McMichael, E.Y. Jones and J.I. Bell (1996). An altered position of the α2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 4, 203-213.
44. D. Housset, G. Mazza, C. Gregoire, C. Piras, B. Malissen and J.C. Fontecilla-Camps (1997). The three-dimensional structure of a T-cell antigen receptor VαVβ heterodimer reveals a novel arrangement of the Vβ domain. EMBO J. 16, 4205-4216.
45. J.H. Brown, T. Jardetzky, M.A. Saper, B. Samraoui, P.J. Bjorkman and D.C. Wiley (1988). A hypothetical model of the foreign antigen binding site of class II histocompatibility molecules. Nature 332, 845-850.
46. B.P. Babbitt, P.M. Allen, G. Matsueda, E. Harber and E.R. Unanue (1985). Binding of immunogenic peptides to Ia histocompatibility molecules. Nature 317, 359-361.
47. S. Buus, A. Sette, S.M. Colon, C. Miles and H.M. Grey (1987). The relation between major histocompatibility complex (MHC) restriction and the capacity of Ia to bind immunogenic peptides. Science 235, 1353-1366.
48. O. Rötzschke and K. Falk (1994). Origin, structure and motifs of naturally processed MHC class II ligands. Curr. Opin. Immunol. 6, 45-51.
49. P.J. Fairchild, H. Pope and D.C. Wraith (1996). The nature of cryptic epitopes within the self-antigen myelin basic protein. Int. Immunol. 8, 1035-1043.
50. L.J. Stern, J.H. Brown, T.S. Jardetzky, J.C. Gorga, R.G. Urban, J.L. Strominger and D.C. Wiley (1994). Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 368, 215-221.
51. M. Srinivasan, S.Z. Domanico, P.T.P. Kaumaya and S.K. Pierce (1993). Peptides of 23 residues or greater are required to stimulate a high affinity class II-restricted T cell response. Eur. J. Immunol. 23, 1011-1016.
52. C.P. Muller, W. Ammerlaan, B. Fleckenstein, S. Krauss, H. Kalbacher, F. Schneider, G. Jung and K.-H. Wiesmüller (1996). Activation of T cells by the ragged tail of MHC class II-presented peptides of the measles virus fusion protein. Int. Immunol. 8, 445-456.
53. A.Y. Rudensky, P. Preston-Hurlburt, S.-C. Hong, A. Barlow and C.A. Janeway (1991). Sequence analysis of peptides bound to MHC class II molecules. Nature 353, 622-627.
54. R.M. Chizc, R.G. Urban, W.S. Lane, J.C. Gorga, L.J. Stem, D.A.A. Vignali and J.L. Strominger (1992). Predominant naturally-processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size. Nature 358, 764-768.
55. d. Science 256, 1817-1820.
56. A.Y. Rudensky, P. Preston-Hurlburt, B.K. Al-Ramadi, J. Rothbard and C.A. Janeway (1992). Truncation variants of peptides isolated form MHC class II molecules suggest sequence motifs. Nature 359, 429-431.
57. M. Srinivasan, E.W. Marsh and S.K. Pierce (1991). Characterization of naturally-processed antigen bound to major histocompatibility complex class II molecules. Proc. Natl. Acad. Sci. USA 88, 7928-7932.
58. D.A.A. Vignali and J.L. Strominger (1994). Amino acid residues that flank core peptide epitopes and the extracellular domains of CD4 modulate differential signaling through the T cell receptor. J. Exp. Med. 179, 1945-1956.
59. T.S. Jardetzky, J.C. Gorga, R. Busch, J. Rothbard, J.L. Strominger and D.C. Wiley (1990). Peptide binding to HLA-DR1: A peptide with most residues substituted to alanine retains MHC binding. EMBO J. 9, 1797-1803.
60. J. Hammer, B. Tabacs and F. Sinigaglia (1992). Identification of a motif for HLA-DR1 binding peptides using M13 display libraries. J. Exp. Med. 176, 1007-1013.
61. F. Sinigaglia and J. Hammer (1994). Defining rules for the peptide-MHC class II interaction. Curr. Opin. Immunol. 6, 52-56.
62. J.I. Krieger, R.W. Karr, H.M. Grey, W-Y. Yu, D O'Sullivan, L. Batovsky, Z.-L. Zheng, S.M. Colon, F.C.A. Gaeta, J. Sidney, M. Albertson, M.-F. Del Guercio, R.W. Chesnut and A. Sette (1991). Single amino acid changes in DR and antigen define critical residues for peptide MHC binding and T cell recognition. J. Immunol. 146, 2331-2340.
63. T.S. Jardetzky, J.H. Brown, J.C. Gorga, J.J. Stern, R.G. Urban, J.L. Strominger and D.C. Wiley (1996). Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides. Proc. Natl. Acad. Sci. USA 93, 734-738.
64. D.H. Fremont, W.A. Hendrickson, P. Marrack and J. Kappler (1996). Structure of an MHC class II molecule with covalently bound single peptides. Science 272, 1001-1004.
65. I.A. Wilson (1996). Another twist to MHC-peptide recognition. Science 272, 973-974.
66. D.R. Madden (1995). The three-dimensional structure of peptide-MHC complexes. Annu. Rev. Immunol. 13, 587-622.
67. H. Kropshofer, H. Max, C.A. Muller, F. Hesse, S. Stevanovic, G. Jung and H. Kalbacher (1992). Self peptide released from class II HLA-DR1 exhibits a hydrophobic two-residue contact motif. J. Exp. Med. 175, 1799-1803.
68. D. O'Sullivan, T. Arrhenius, J. Sidney, M.-F. Del Guercio, M. Albertson, M. Wall, C. Oseroff, S. Southwood, S.M. Colon, F.C.A. Gaeta and A. Sette (1991). On the interaction of promiscuous peptides with different DR alleles. Identification of common structural motifs. J. Immunol. 147, 2663-2669.
69. P. Panina-Bordignon, A. Tan, A. Terrnijtelen, S. Demotz, G. Corradin and A. Lanzavecchia (1989). Universally immunogenic T cell epitopes: Promiscuous binding to human MHC class II and promiscuous recognition by T cells. Eur. J. Immunol. 19, 2237-2242.
70. J.M. Riberdy, J.R. Newcomb, M.J. Surman, J.A. Barbosa and P. Cresswell (1992). HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides. Nature 360, 474-477.
71. N. Bangia and T.H. Watts (1995). Evidence for invariant chain 85-101 (CLIP) binding in the antigen binding site of MHC class II molecules. Int. Immunol. 7, 1585-1591.
72. F. Sinigaglia and J. Hammer (1995). Motifs and supermotifs for MHC class II binding peptides. J. Exp. Med. 18, 449-451.
73. G. Malcherek, V. Gnau, G. Jung, H.-G Rammensee and A. Melms (1995). Supermotifs enable natural invariant chain-derived peptides to interact with many major histocompatibility complex-class II molecules. J. Exp. Med. 181, 527-536.
74. A.M. Gautam, C. Pearson, V. Quinn, H.O. McDevitt and P.J. Milburn (1995). Binding of an invariant-chain peptide, CLIP, to I-A major histocompatibility complex class II molecules. Proc. Natl. Acad. Sci USA 92, 335-339.
75. P. Ghosh, M. Amaya, E. Mellins and D.C. Wiley (1995). The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature 378, 457-462.
76. S.M. Weenink, P.J. Milburn and A.M. Gautam (1997). A continuous central motif of invariant chain peptides, CLIP, is essential for binding to various I-A MHC class II molecules. Int. Immunol. 9, 317-325.
77. S. Sadegh-Nasseri and R.N. Germain (1991). A role for peptide in determining MHC class II structure. Nature 353, 167-170.
78. S. Sadegh-Nasseri and R.N. Germain (1992). How MHC class II molecules work: Peptide-dependent completion of protein folding. Immunol. Today 13, 43-46.
79. A. Sette and H.M. Grey (1992). Chemistry of peptide interaction with MHC proteins. Curr. Opin. Immunol. 4, 79-86.
80. C.A. Nelson, S.J. Petzold and E.R. Unanue (1994). Peptides determine the lifespan of MHC class II molecules in the antigen-presenting cell. Nature 371, 250-252.
81. P.J. Fairchild, C.J. Thorpe, P.J. Travers and D.C. Wraith (1994). Modulation of the immune response with T-cell epitopes: The ultimate goal for specific immunotherapy of autoimmune disease. Immunology 81, 487-496.
82. P.J. Fairchild (1997). Altered peptide ligands: Prospects of immune intervention in autoimmune disease. Eur. J. Immunogenet. 24, 155-167.