An autonomous CDR3δ is sufficient for recognition of the nonclassical MHC class I molecules T10 and T22 by γδ T cells

Nature Immunology

Volumn 9, Issue 7, 2008, Pages 777-784

  Adams, Erin J ^a   Strop, Pavel ^b   Shin, Sunny ^b   Chien, Yueh Hsiu ^b   Garcia, K Christopher ^b  

^a UNIVERSITY OF CHICAGO   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CD38 ANTIGEN; HLA B ANTIGEN; T LYMPHOCYTE RECEPTOR DELTA CHAIN; T LYMPHOCYTE RECEPTOR GAMMA CHAIN; T22 ANTIGEN; HLA ANTIGEN CLASS 1; LYMPHOCYTE ANTIGEN RECEPTOR;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ANTIGEN FUNCTION; ANTIGEN RECOGNITION; ANTIGEN SPECIFICITY; ANTIGEN STRUCTURE; ARTICLE; BINDING AFFINITY; BINDING KINETICS; COMPLEMENTARITY DETERMINING REGION; CONTROLLED STUDY; IMMUNOREACTIVITY; LIGAND BINDING; MOLECULAR RECOGNITION; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN POLYMORPHISM; SEQUENCE HOMOLOGY; ANIMAL; BINDING SITE; CHEMISTRY; CIRCULAR DICHROISM; GENETICS; HUMAN; IMMUNOLOGY; LYMPHOCYTE ACTIVATION; METABOLISM; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; STRUCTURE ACTIVITY RELATION; SURFACE PLASMON RESONANCE; T LYMPHOCYTE; T LYMPHOCYTE SUBPOPULATION;

ANIMALS; BINDING SITES; CIRCULAR DICHROISM; COMPLEMENTARITY DETERMINING REGIONS; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; LYMPHOCYTE ACTIVATION; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA; STRUCTURE-ACTIVITY RELATIONSHIP; SURFACE PLASMON RESONANCE; T-LYMPHOCYTE SUBSETS; T-LYMPHOCYTES;

EID: 45549106387     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni.1620     Document Type: Article

References (49)

1. Adams, E.J., Chien, Y.H. & Garcia, K.C. Structure of a γδ T cell receptor in complex with the nonclassical MHC T22. Science 308 227-231 (2005).
2. Allison, T.J., Winter, C.C., Fournie, J.J., Bonneville, M. & Garboczi, D.N. Structure of a human γδ T-cell antigen receptor. Nature 411, 820-824 (2001).
3. Battistini, L. et al. Phenotypic and cytokine analysis of human peripheral blood γδ T cells expressing NK cell receptors. J. Immunol. 159, 3723-3730 (1997).
4. Spada, F.M. et al. Self-recognition of CD1 by γ/δ T cells: implications for innate immunity. J. Exp. Med. 191, 937-948 (2000).
5. Ferrick, D.A. et al. Differential production of interferon-γ and interleukin-4 in response to Th1- and Th2-stimulating pathogens by γδ T cells in vivo. Nature 373, 255-257 (1995).
6. Wen, L. et al. Primary γδ cell clones can be defined phenotypically and functionally as Th1/Th2 cells and illustrate the association of CD4 with Th2 differentiation. J. Immunol. 160 1965-1974 (1998).
7. Brenner, M.B. et al. Identification of a putative second T-cell receptor. Nature 322, 145-149 (1986).
8. Fisch, P. et al. Gamma/delta T cell clones and natural killer cell clones mediate distinct patterns of non-major histocompatibility complex-restricted cytolysis. J. Exp. Med. 171, 1567-1579 (1990).
9. Wright, A. et al. Cytotoxic T lymphocytes specific for self tumor immunoglobulin express T cell receptor δ chain. J. Exp. Med. 169, 1557-1564 (1989).
10. Jameson, J. et al. A role for skin γδ T cells in wound repair. Science 296, 747-749 (2002).
11. Brandes, M., Willimann, K. & Moser, B. Professional antigen-presentation function by human γδ T cells. Science 309, 264-268 (2005).
12. Kapp, J.A., Kapp, L.M. & McKenna, K.C. γδ T cells play an essential role in several forms of tolerance. Immunol. Res. 29, 93-102 (2004).
13. De Libero, G. Tissue distribution, antigen specificity and effector functions of γδ T cells in human diseases. Springer Semin. Immunopathol. 22, 219-238 (2000).
14. Garcia, K.C. & Adams, E.J. Haw the T cell receptor sees antigen-a structural view. Cell 122, 333-336 (2005).
15. Rudolph, M.G. & Wilson, I.A. The specificity of TCR/pMHC interaction. Curr. Opin. Immunol. 14, 52-65 (2002).
16. Davies, D.R. & Cohen, G.H. Interactions of protein antigens with antibodies. Proc. Natl. Acad. Sci. USA 93, 7-12 (1996).
17. Porcelli, S. et al. Recognition of cluster of differentiation 1 antigens by human CD4-CD8-cytolytic T lymphocytes. Nature 341 447-450 (1989).
18. Schild, H. et al. The nature of major histocompatibility complex recognition by γδ T cells. Cell 76, 29-37 (1994).
19. Weintraub, B.C., Jackson, M.R. & Hedrick, S.M. Gamma delta T cells can recognize nonclassical MHC in the absence of conventional antigenic peptides. J. Immunol. 153, 3051-3058 (1994).
20. Groh, V., Steinle, A., Bauer, S. & Spies, T. Recognition of stress-induced MHC molecules by intestinal epithelial γδ T cells. Science 279, 1737-1740 (1998).
21. Scotet, E. et al. Tumor recognition following Vγ9Vδ2 T cell receptor interactions with a surface F1-ATPase-related structure and apolipoprotein A-I. Immunity 22, 71-80 (2005).
22. Johnson, R.M. et al. A murine CD4-, CD8- T cell receptor-γδ T lymphocyte clone specific for herpes simplex virus glycoprotein I. J. Immunol. 148, 983-988 (1992).
23. Elliott, J.F., Rock, E.P., Patten, P.A., Davis, M.M. & Chien, Y.H. The adult T-cell receptor δ-chain is diverse and distinct from that of fetal thymocytes. Nature 331, 627-631 (1988).
24. Crowley, M.P. et al. A population of murine γδ T cells that recognize an inducible MHC class Ib molecule. Science 287, 314-316 (2000).
25. - T lymphocytes. J. Exp. Med. 168, 1899-1916 (1988).
26. Bonneville, M. et al. Recognition of a self major histocompatibility complex TL region product by γδ T-cell receptors. Proc. Natl. Acad. Sci. USA 86, 5928-5932 (1989).
27. Ito, K. et al. Recognition of the product of a novel MHC TL region gene (27b) by a mouse γδ T cell receptor. Cell 62, 549-561 (1990).
28. Shin, S. et al. Antigen recognition determinants of γδ T cell receptors. Science 308, 252-255 (2005).
29. Li, H. et al. Structure of the Vδ domain of a human γδ T-cell antigen receptor. Nature 391, 502-506 (1998).
30. Maynard, J. et al. Structure of an autoimmune T cell receptor complexed with class II peptide-MHC: Insights into MHC bias and antigen specificity. Immunity 22, 81-92 (2005).
31. Moriwaki, S., Korn, B.S., Ichikawa, Y., van Kaer, L. & Tonegawa, S. Amino acid substitutions in the floor of the putative antigen-binding site of H-2T22 affect recognition by a γδ T-cell receptor. Proc. Natl. Acad. Sci. USA 90, 11396-11400 (1993).
32. Padian, E. Anatomy of the antibody molecule. Mol. Immunol. 31 169-217 (1994).
33. Garboczi, D.N. et al. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384, 134-141 (1996).
34. Reiser, J.B. et al. A T cell receptor CDR3β loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex. Immunity 16, 345-354 (2002).
35. Huang, C.C. et al. Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4. Science 317, 1930-1934 (2007).
36. Kodandapani, R., Veerapandian, B., Kunicki, T.J. & Ely, K.R. Crystal structure of the OPG2 Fab. An antireceptor antibody that mimics an RGD cell adhesion site. J. Biol. Chem. 270, 2268-2273 (1995).
37. Stanfield, R.L., Dooley, H., Flajnik, M.F. & Wilson, I.A. Crystal structure of a shark single-domain antibody V region in complex with lysozyme. Science 305, 1770-1773 (2004).
38. Matis, L.A., Cron, R. & Bluestone, J.A. Major histocompatibility complex-linked specificity of γδ receptor-bearing T lymphocytes. Nature 330, 262-264 (1987).
39. Lee, C.V. et al. High-affinity human antibodies from phage-displayed synthetic Fab libraries with a single framework scaffold. J. Mol. Biol. 340, 1073-1093 (2004).
40. Holler, P.D. et al. In vitro evolution of a T cell receptor with high affinity for peptide/MHC. Proc. Natl. Acad. Sci. USA 97 5387-5392 (2000).
41. Patten, P.A. et al. Transfer of putative complementarity-determining region loops of T cell receptor V domains confers toxin reactivity but not peptide/MHC specificity. J. Immunol. 150, 2281-2294 (1993).
42. Presta, L.G. et al. Humanization of an antibody directed against IgE. J. Immunol. 151, 2623-2632 (1993).
43. Feng, D., Bond, C.J., Ely, L.K., Maynard, J. & Garcia, K.C. Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'. Nat. Immunol. 8, 975-983 (2007).
44. Huseby, E.S. et al. How the T cell repertoire becomes peptide and MHC specific. Cell 122, 247-260 (2005).
45. Hewitt, E.W. The MHC class I antigen presentation pathway: Strategies for viral immune evasion. Immunology 110, 163-169 (2003).
46. Maynard, J. et al. High-level bacterial secretion of single-chain αβ T-cell receptors. J. Immunol. Methods 306, 51-67 (2005).
47. Minor, D.L. Jr. & Kim, P.S. Measurement of the β-sheet-forming propensities of amino acids. Nature 367, 660-663 (1994).
48. Crowley, M.P., Reich, Z., Mavaddat, N., Altman, J.D. & Chien, Y. The recognition of the nonclassical major histocompatibility complex (MHC) class I molecule, T10, by the γδ T cell, G8. J. Exp. Med. 185 1223-1230 (1997).
49. Wingren, C., Crowley, M.P., Degano, M., Chien, Y. & Wilson, I.A. Crystal structure of a γδ T cell receptor ligand T22: A truncated MHC-like fold. Science 287, 310-314 (2000).