Recognition of open conformers of classical MHC by chaperones and monoclonal antibodies

Immunological Reviews

Volumn 207, Issue , 2005, Pages 100-111

  Hansen, Ted H ^a   Lybarger, Lonnie ^b   Yu, Lawrence ^a   Mitaksov, Vesselin ^a   Fremont, Daved H ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HLA DM ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MONOCLONAL ANTIBODY; TAPASIN;

HUMAN; MAJOR HISTOCOMPATIBILITY COMPLEX; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW;

ANIMALS; ANTIBODIES, MONOCLONAL; ANTIPORTERS; HUMANS; IMMUNOGLOBULINS; MAJOR HISTOCOMPATIBILITY COMPLEX; MEMBRANE TRANSPORT PROTEINS; MOLECULAR CHAPERONES; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY;

EID: 26244456282     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0105-2896.2005.00315.x     Document Type: Review

References (101)

1. Bouvier M, Wiley DC. Structural characterization of a soluble and partially folded class I major histocompatibility heavy chain/beta 2m heterodimer. Nat Struct Biol 1998;5:377-384.
2. Bouvier M. Accessory proteins and the assembly of human class I MHC molecules: a molecular and structural perspective. Mol Immunol 2003;39:697-706.
3. Williams A, Peh CA, Elliott T. The cell biology of MHC class I antigen presentation. Tissue Antigens 2002;59:3-17.
4. Jensen PE, et al. HLA-DM and the MHC class II antigen presentation pathway. Immunol Res 1999;20:195-205.
5. Vogt AB, Kropshofer H, Hammerling GJ. How HLA-DM affects the peptide repertoire bound to HLA-DR molecules. Hum Immunol 1997;54:170-179.
6. Alfonso C, Karlsson L. Nonclassical MHC class II molecules. Annu Rev Immunol 2000;18:113-142.
7. Kropshofer H, Hammerling GJ, Vogt AB. The impact of the non-classical MHC proteins HLA-DM and HLA-DO on loading of MHC class II molecules. Immunol Rev 1999;172:267-278.
8. Busch R, Mellins ED. Developing and shedding inhibitions: how MHC class II molecules reach maturity. Curr Opin Immunol 1996;8:51-58.
9. Williams AP, et al. Optimization of the MHC class I peptide cargo is dependent on tapasin. Immunity 2002;16:509-520.
10. Howarth M, et al. Tapasin enhances MHC class I peptide presentation according to peptide half-life. Proc Natl Acad Sci USA 2004;101:11737-11742.
11. d class I major histocompatibility complex molecules determines their antigenic structure. J Exp Med 1991;173:449-459.
12. d in cell lysates and the cell surface. J Exp Med 1992;175:191-202.
13. d molecules at the cell surface. J Exp Med 1993;178:2035-2046.
14. Smith JD, et al. Characterization of class I MHC folding intermediates and their disparate interactions with peptide and beta 2-microglobulin. Mol Immunol 1995;32:531-540.
15. Yu YY, et al. Definition and transfer of a serological epitope specific for peptide-empty forms of MHC class I. Int Immunol 1999;11:1897-1906.
16. Machold RP, Ploegh HL. Intermediates in the assembly and degradation of class I major histocompatibility complex (MHC) molecules probed with free heavy chain-specific monoclonal antibodies. J Exp Med 1996;184:2251-2259.
17. Sernee MF, Ploegh HL, Schust DJ. Why certain antibodies cross-react with HLA-A and HLA-G: epitope mapping of two common MHC class I reagents. Mol Immunol 1998;35:177-188.
18. Benjamin RJ, et al. Polymorphic specificity of Q1/28, a monoclonal antibody that preferentially reacts with free class I heavy chains. Immunogenetics 1992;37:73-76.
19. Madrigal JA, et al. Molecular definition of a polymorphic antigen (LA45) of free HLA-A and -B heavy chains found on the surfaces of activated B and T cells. J Exp Med 1991;174:1085-1095.
20. Setini A, et al. Distinctive features of the alpha 1-domain alpha helix of HLA-C heavy chains free of beta 2-microglobulin. Hum Immunol 1996;46:69-81.
21. LaPan KE, Klapper DG, Frelinger JA. Production and characterization of two new mouse monoclonal antibodies reactive with denatured mouse class II beta chains. Hybridoma 1992;11:217-223.
22. Santambrogio L, et al. Abundant empty class II MHC molecules on the surface of immature dendritic cells. Proc Natl Acad Sci USA 1999;96:15050-15055.
23. Sato AK, et al. Determinants of the peptide-induced conformational change in the human class II major histocompatibility complex protein HLA-DR1. J Biol Chem 2000;275:2165-2173.
24. Carven GJ, et al. Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding. J Biol Chem 2004;279:16561-16570.
25. Townsend A, et al. Association of class I major histocompatibility heavy and light chains induced by viral peptides. Nature 1989;340:443-448.
26. d class I MHC molecule. Nature 1990;344:439-441.
27. Chiu NM, et al. The majority of H2-M3 is retained intracellularly in a peptide-receptive state and traffics to the cell surface in the presence of N-formylated peptides. J Exp Med 1999;190:423-434.
28. Townsend A, et al. Assembly of MHC class I molecules analyzed in vitro. Cell 1990;62:285-295.
29. Elliott T, et al. Peptide-induced conformational change of the class I heavy chain. Nature 1991;351:402-406.
30. Rigney E, et al. A soluble major histocompatibility complex class I peptide-binding platform undergoes a conformational change in response to peptide epitopes. J Biol Chem 1998;273:14200-14204.
31. Springer S, et al. Fast association rates suggest a conformational change hi the MHC class I molecule H-2Db upon peptide binding. Biochemistry 1998;37:3001-3012.
32. d serologic recognition. J Immunol 1993;151:5387-5397.
33. Carreno BM, et al. TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man. J Immunol 1995;155:4726-4733.
34. Carreno BM, et al. A glycosylated and phosphatidylinositol-anchored MHC class I molecules are associated with calnexin. Evidence implicating the class I-connecting peptide segment in calnexin association. J Immunol 1995;154:5173-5180.
35. Harris MR, et al. Association of ERp57 with mouse MHC class I molecules is tapasin dependent and mimics that of calreticulin and not calnexin. J Immunol 2001;166:6686-6692.
36. Harris MR, et al. Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I. J Immunol 1998;160:5404-5409.
37. Solheim JC, et al. Prominence of beta 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 1997;158:2236-2241.
38. Yu YY, et al. Cutting edge: single-chain trimers of MHC class I molecules form stable structures that potently stimulate antigen-specific T cells and B cells. J Immunol 2002;168:3145-3149.
39. Lybarger L, et al. Enhanced immune presentation of a single-chain major histocompatibility complex class I molecule engineered to optimize linkage of a C-terminally extended peptide. J Biol Chem 2003;278:27105-27111.
40. d molecules and of GFP-TAP1 reports on the assembly and retention of these molecules in the endoplasmic reticulum. Immunity 1999;11:231-240.
41. Williams DB, Swiedler SJ, Hart GW. Intracellular transport of membrane glycoproteins: two closely related histocompatibility antigens differ in their rates of transit to the cell surface. J Cell Biol 1985;101:725-734.
42. d are influenced by its amino terminus. J Immunol 1986;137:916-923.
43. Neisig A, et al. Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing. J Immunol 1996;156:3196-3206.
44. d molecules share common tapasin dependencies as determined using a novel epitope tag. J Immunol 2000;165:5656-5663.
45. Lybarger L, et al. Tapasin enhances peptide-induced expression of H2-M3 molecules, but is not required for the retention of open conformers. J Immunol 2001;167:2097-2105.
46. Harris MR, et al. Interactions of HLA-B27 with the peptide loading complex as revealed by heavy chain mutations. Int Immunol 2001;13:1275-1282.
47. McPhalen CA, et al. Domain closure in mitochondrial aspartate aminotransferase. J Mol Biol 1992;227:197-213.
48. Gerstein M, Chothia C. Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase. J Mol Biol 1991;220:133-149.
49. Peh CA, et al. HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading. Immunity 1998;8:531-542.
50. Neefjes JJ, Ploegh HL. Allele and locus-specific differences in cell surface expression and the association of HLA class I heavy chain with beta 2-microglobulin: differential effects of inhibition of glycosylation on class I subunit association. Eur J Immunol 1988;18:801-810.
51. Braud VM, Allan DS, McMichael AJ. Functions of nonclassical MHC and non-MHC-encoded class I molecules. Curr Opin Immunol 1999;11:100-108.
52. Miley MJ, et al. Biochemical features of the MHC-related protein 1 consistent with an immunological function. J Immunol 2003;170:6090-6098.
53. Lindahl KF, et al. H2-M3, a full-service class Ib histocompatibility antigen. Annu Rev Immunol 1997;15:851-879.
54. Chun T, et al. Functional roles of TAP and tapasin in the assembly of M3-N-formylated peptide complexes. J Immunol 2001;167:1507-1514.
55. 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.
56. Grandea AG, Van Kaer L. Tapasin: an ER chaperone that controls MHC class I assembly with peptide. Trends Immunol 2001;22:194-199.
57. Schoenhals GJ, et al. Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cells. EMBO J 1999;18:743-753.
58. Barnden MJ, et al. Tapasin-mediated retention and optimization of peptide ligands during the assembly of class I molecules. J Immunol 2000;165:322-330.
59. Grandea AGIII, , et al. Impaired assembly yet normal trafficking of MHC class I molecules in Tapasin mutant mice. Immunity 2000;13:213-222.
60. Lehner PJ, Surman MJ, Cresswell P. Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line .220. Immunity 1998;8:221-231.
61. Braud VM, et al. TAP- and tapasin-dependent HLA-E surface expression correlates with the binding of an MHC class I leader peptide. Curr Biol 1998;8:1-10.
62. 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.
63. Hildebrand WH, et al. HLA class I polymorphism has a dual impact on ligand binding and chaperone interaction. Hum Immunol 2002;63:248-255.
64. Park B, et al. A single polymorphic residue within the peptide-binding cleft of MHC class I molecules determines spectrum of tapasin dependence. J Immunol 2003;170:961-968.
65. Zernich D, et al. Natural HLA class I polymorphism controls the pathway of antigen presentation and susceptibility to viral evasion. J Exp Med 2004;200:13-24.
66. Elliott T. How does TAP associate with MHC class I molecules? Immunol Today 1997;18:375-379.
67. 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.
68. Kulig K, et al. 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.
69. Connolly JM, et al. Recognition by CD8 on cytotoxic T lymphocytes is ablated by several substitutions in the class I alpha 3 domain: CD8 and the T-cell receptor recognize the same class I molecule. Proc Natl Acad Sci USA 1990;87:2137-2141.
70. Connolly JM, et al. The Lyt-2 molecule recognizes residues in the class I alpha 3 domain in allogeneic cytotoxic T cell responses. J Exp Med 1988;168:325-341.
71. Bangia N, et al. The N-terminal region of tapasin is required to stabilize the MHC class I loading complex. Eur J Immunol 1999;29:1858-1870.
72. Peace-Brewer AL, et al. 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.
73. Lewis JW, et al. Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP. Curr Biol 1996;6:873-883.
74. Yu YY, et al. An extensive region of an MHC class I alpha 2 domain loop influences interaction with the assembly complex. J Immunol 1999;163:4427-4433.
75. Miyazaki J, et al. Expression and function of a nonglycosylated major histocompatibility class I antigen. J Exp Med 1986;163:856-871.
76. Stam NJ, Spits H, Ploegh HL. Monoclonal antibodies raised against denatured HLA-B locus heavy chains permit biochemical characterization of certain HLA-C locus products. J Immunol 1986;137:2299-2306.
77. Stam NJ, et al. HLA-A- and HLA-B-specific monoclonal antibodies reactive with free heavy chains in western blots, in formalin-fixed, paraffin-embedded tissue sections and in cryo-immuno-electron microscopy. Int Immunol 1990;2:113-125.
78. Perosa F, et al. Beta 2-microglobulin-free HLA class I heavy chain epitope mimicry by monoclonal antibody HC-10-specific peptide. J Immunol 2003;171:1918-1926.
79. Beretta A, et al. HIV env glycoprotein shares a cross-reacting epitope with a surface protein present on activated human monocytes and involved in antigen presentation. Eur J Immunol 1987;17:1793-1798.
80. Schnabl E, et al. Activated human T lymphocytes express MHC class I heavy chains not associated with beta 2-microglobulin. J Exp Med 1990;171:1431-1442.
81. Aiuti A, et al. Membrane expression of HLA-Cw4 free chains in activated T cells of transgenic mice. Immunogenetics 1995;42:368-375.
82. Giacomini P, et al. HLA-C heavy chains free of beta2-microglobulin: distribution in normal tissues and neoplastic lesions of non-lymphoid origin and interferon-gamma responsiveness. Tissue Antigens 1997;50:555-566.
83. Martayan A, et al. Biosynthesis of HLA-C heavy chains in melanoma cells with multiple defects in the expression of HLA-A-B-C molecules. Br J Cancer 1999;80:639-649.
84. Blaschitz A, Hutter H, Dohr G. HLA Class I protein expression in the human placenta. Early Pregnancy 2001;5:67-69.
85. Pickl WF, et al. Expression of LA45 reactive beta 2-microglobulin free HLA class I alpha-chains on activated T-cells is regulated by internalization, constitutive and protein kinase C inducible release. Tissue Antigens 1996;48:15-21.
86. Sadegh-Nasseri S, Germain RN. A role for peptide in determining MHC class II structure. Nature 1991;353:167-170.
87. b. Science 1992;257:919-927.
88. Smith KJ, et al. An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 1996;4:203-213.
89. Doebele RC, et al. Determination of the HLA - DM interaction site on HLA-DR molecules. Immunity 2000;13:517-527.
90. Brocke P, et al. HLA-DM, HLA-DO and tapasin: functional similarities and differences. Curr Opin Immunol 2002;14:22-29.
91. Murthy VL, Stern LJ. The class II MHC protein HLA-DR1 in complex with an endogenous peptide: implications for the structural basis of the specificity of peptide binding. Structure 1997;5:1385-1396.
92. Latek RR, et al. Structural basis of peptide binding and presentation by the type I diabetes-associated MHC class II molecule of NOD mice. Immunity 2000;12:699-710.
93. 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 1995;92:2479-2483.
94. Kersh GJ, et al. Structural and functional consequences of altering a peptide MHC anchor residue. J Immunol 2001;166:3345-3354.
95. Apostolopoulos V, et al. Crystal structure of a non-canonical high affinity peptide complexed with MHC class I: a novel use of alternative anchors. J Mol Biol 2002;318:1307-1316.
96. Rudolph MG, et al. The crystal structures of K (bm1) and K (bm8) reveal that subtle changes in the peptide environment impact thermostability and alloreactivity. Immunity 2001;14:231-242.
97. Ostrov DA, et al. How H13 histocompatibility peptides differing by a single methyl group and lacking conventional MHC binding anchor motifs determine self-nonself discrimination. J Immunol 2002;168:283-289.
98. Achour A, et al. The crystal structure of H-2Dd MHC class I complexed with the HIV-1-derived peptide P18-I10 at 2.4A resolution: implications for T cell and NK cell recognition. Immunity 1998;9:199-208.
99. Fremont DH, et al. Crystal structure of I-Ak in complex with a dominant epitope of lysozyme. Immunity 1998;8:305-317.
100. Scott CA, et al. Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues. Immunity 1998;8:319-329.
101. Zhu Y, et al. Crystal structure of MHC class II, I-Ab in complex with a human CLIP peptide: prediction of an I-Ab peptide-binding motif. J Mol Biol 2003;326:1157-1174.