A Three-Domain T Cell Receptor Is Biologically Active and Specifically Stains Cell Surface MHC/Peptide Complexes

Journal of Immunology

Volumn 158, Issue 5, 1997, Pages 2218-2227

  Plaksin, Daniel ^a   Polakova, Katarina ^a,c   McPhie, Peter ^b   Margulies, David H ^a,d  

^a Natl Inst Allerg and Infect Dis   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^c CANCER RESEARCH INSTITUTE   (Slovakia)

^d NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; H2 ANTIGEN; IMMUNOGLOBULIN; LYMPHOCYTE ANTIGEN RECEPTOR; MONOCLONAL ANTIBODY; PEPTIDE;

AMINO ACID SEQUENCE; ANIMAL; ANTIBODY SPECIFICITY; ANTIGEN ANTIBODY REACTION; ARTICLE; BIOSYNTHESIS; CHEMISTRY; CIRCULAR DICHROISM; HYBRIDOMA; IMMUNOLOGY; LYMPHOCYTE ACTIVATION; MOLECULAR GENETICS; MOUSE; NUCLEOTIDE SEQUENCE; PHYSIOLOGY; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STAINING; T LYMPHOCYTE;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; ANTIBODY SPECIFICITY; ANTIGEN-ANTIBODY REACTIONS; BASE SEQUENCE; CIRCULAR DICHROISM; EPITOPES; H-2 ANTIGENS; HYBRIDOMAS; IMMUNOGLOBULINS; LYMPHOCYTE ACTIVATION; MICE; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, ANTIGEN, T-CELL; STAINING AND LABELING; T-LYMPHOCYTES;

EID: 0031091745     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (73)

1. Hedrick, S. M., L. A. Matis, T. T. Hecht, L. E. Samelson, D. L. Longo, E. Heber-Katz, and R. H. Schwartz. 1982. The fine specificity of antigen and Ia determinant recognition by T cell hybridoma clones specific for pigeon cytochrome c. Cell 30:141.
2. Jorgensen, J. L., P. A. Reay, E. W. Ehrich, and M. M. Davis. 1992. Molecular components of T-cell recognition. Annu. Rev. Immunol. 10:835.
3. Jorgensen, J. L., U. Esser, B. F. de St. Groth, P. A. Reay, and M. M. Davis. 1992. Mapping T-cell receptor-peptide contacts by variant peptide immunization of single-chain transgenics. Nature 355:224.
4. Corr, M., A. E Slanetz, L. F. Boyd, M. T. Jelonek, S. Khilko, B. K. al-Ramadi, Y. S. Kim, S. E. Maher, A. L. Bothwell, and D. H. Margulies. 1994. T cell receptor-MHC class I peptide interactions: affinity, kinetics, and specificity. Science 265:946.
5. Sant'Angelo, D. B., G. Waterbury, P. Preston-Hurlburt, S. T. Yoon, R. Medzhitov, S. C. Hong, and C. A. Janeway, Jr. 1996. The specificity and orientation of a TCR to its peptide-MHC class II ligands. Immunity 4:367.
6. Alam, S. M., P. J. Travers, J. L. Wung, W. Nasholds, S. Redpath, S. C. Jameson, and N. R. J. Gascoigne. 1996. T cell receptor affinity and thymocyte positive selection. Nature 381:616.
7. Lin, A. Y., B. Devaux, A. Green, C. Sagerstrom, J. F. Elliott, and M. M. Davis. 1990. Expression of T cell antigen receptor heterodimers in a lipid-linked form. Science 249:677.
8. Slanetz, A. E., and A. L. Bothwell. 1991. Heterodimeric, disulfide-linked α/βT cell receptors in solution. Eur. J. Immunol. 21:179.
9. Gregoire, C., N. Rebai, F. Schweisguth, A. Necker, G. Mazza, N. Auphan, A. Millward, A. M. Schmitt-Verhulst, and B. Malissen. 1991. Engineered secreted T-cell receptor αβ heterodimers. Proc. Natl. Acad. Sci. USA 88:8077.
10. Weber, S., 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.
11. Engel, I., T. H. Ottenhoff, and R. D. Klausner. 1992. High-efficiency expression and solubilization of functional T cell antigen receptor heterodimers. Science 256:1318.
12. Chang, H. C., Z. Z. Bao, Y. Yao, A. G. D. Tse, E. C. Goyarts, M. Madsen, E. Kawasaki, P. P. Brauer, J. C. Sacchettini, S. G. Nathenson, and E. L. Reinherz. 1994. A general method for facilitating heterodimeric pairing between two proteins: application to expression of α and β T-cell receptor extracellular segments. Proc. Natl. Acad. Sci. USA 91:11408.
13. Kappler, J., J. White, H. Kozono, J. Clements, and P. Marrack. 1994. Binding of a soluble αβ T-cell receptor to superamigen/major histocompatibility complex ligands. Proc. Natl. Acad. Sci. USA 91:8462.
14. Strong, R. K., D. M. Penny, R. M. Feldman, L. P. Weiner, J. J. Boniface, M. M. Davis, and P. J. Bjorkman. 1994. Engineering and expression of a secreted murine TCR with reduced N-linked glycosylation. J. Immunol. 153:4111.
15. + cells. J. Immunol. 145:1324.
16. Gascoigne, N. R., and K. T. Ames. 1991. Direct binding of secreted T-cell receptor β chain to superantigen associated with class II major histocompatibility complex protein. Proc. Natl. Acad. Sci. USA 88:613.
17. Ward, E. S. 1992. Secretion of T cell receptor fragments from recombinant Escherichia coli cells. J. Mol. Biol. 224:885.
18. Plaksin, D., S. Chacko, P. McPhie, A. Bax, E. A. Padlan, and D. H. Margulies. 1996. A T cell receptor Vα domain expressed in bacteria: does it dimerize in solution? J. Exp. Med. 184:1251.
19. Kurucz, I., C. R. Jost, A. J. George, S. M. Andrew, and D. M. Segal. 1993. A bacterially expressed single-chain Fv construct from the 2B4 T-cell receptor. Proc. Natl. Acad. Sci. USA 90:3830.
20. Novotny, J., R. K. Ganju, S. T. Smiley, R. E. Hussey, M. A. Luther, M. A. Recny, R. F. Siliciano, and E. L. Reinherz. 1991. A soluble, single-chain T-cell receptor fragment endowed with antigen-combining properties. Proc. Natl. Acad. Sci. USA 88:8646.
21. Soo Hoo, W. F., M. J. Lacy, L. K. Denzin, E. W. Voss, Jr., K. D. Hardman, and D. M. Kranz. 1992. Characterization of a single-chain T-cell receptor expressed in Escherichia coli. Proc. Natl. Acad. Sci. USA 89:4759.
22. Wulfing, C., and A. Pluckthun. 1994. Correctly folded T-cell receptor fragments in the periplasm of Escherichia coli: influence of folding catalysts. J. Mol. Biol. 242:655.
23. Hilyard, K. L., H. Reyburn, S. Chung, J. I. Bell, and J. L. Strominger. 1994. Binding of soluble natural ligands to a soluble human T-cell receptor fragment produced in Escherichia coli. Proc. Natl. Acad. Sci. USA 91:9057.
24. Bentley, G. A., G. Boulot, K. Karjalainen, and R. A. Mariuzza. 1995. Crystal structure of the beta chain of a T cell antigen receptor. Science 267:1984.
25. Chung, S., K. W. Wucherpfennig, S. M. Friedman, D. A. Hafler, and J. L. Strominger. 1994. Functional three-domain single-chain T-cell receptors. Proc. Natl. Acad. Sci. USA 91:12654.
26. Takahashi, H., J. Cohen, A. Hosmalin, K. Cease, R. Houghten, J. Cornette, C. DeLisi, B. Mosys, R. Germain, and J. Berzofsky. 1988. An immunodominant epitope of the human immunodeficiency virus envelope glycoprotein gp160 recognized by class I major histocompatibility complex molecule-restricted murine cytotoxic T lymphocytes. Proc. Natl. Acad. Sci. USA 85:3105.
27. Shirai, M., C. D. Pendleton, and J. A. Berzofsky. 1992. Broad recognition of cytotoxic T cell epitopes from the HIV-1 envelope protein with multiple class I histocompatibility molecules. J. Immunol. 148:1657.
28. Kozlowski, S., T. Takeshita, W. H. Boehncke, H. Takahashi, L. F. Boyd, R. N. Germain, J. A. Berzofsky, and D. H. Margulies. 1991. Excess β2 microglobulin promoting functional peptide association with purified soluble class I MHC molecules. Nature 349:74.
29. Barth, R. K., B. S. Kim, N. C. Lan, T. Hunkapiller, N. Sobieck, A. Winoto, H. Gershenfeld, C. Okada, D. Hansburg, I. L. Weissman, and L. Hood. 1985. The murine T-cell receptor uses a limited repertoire of expressed Vβ gene segments. Nature 316:517.
30. Chien, Y. H., R. J. Gascoigne, J. Kavaler, N. E. Lee, and M. M. Davis. 1984. Somatic recombination in a murine T-cell receptor gene. Nature 309:322.
31. d exploits a four residue peptide binding motif. J. Exp. Med. 178:1877.
32. Studier, F. W., A. H. Rosenberg, J. J. Dunn, and J. W. Dubendorff. 1990. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enymol. 185:60.
33. Chaudhary, V. K., C. Queen, R. P. Junghans, T. A. Waldmann, D. J. FitzGerald, and I. Pastan. 1989. A recombinant immunotoxin consisting of two antibody variable domains fused to Pseudomonas exotoxin. Nature 339:394.
34. s: sequence motif, quantitative binding, and molecular modeling of the complex. J. Exp. Med. 176:1681.
35. k and T cell receptor Vα haplotypes: determination with a Vα2-specific monoclonal antibody. Eur. J. Immunol. 22:399.
36. Okada, C., B. Holzmann, D. Guidos, E. Palmer, and I. Weissman. 1990. Characterization of a rat monoclonal antibody specific for a determinant encoded by the Vβ7 gene segment. J. Immunol. 144:3473.
37. Kubo, R. T., W. Born, J. W. Kappler, P. Marrack, and M. Pigeon. 1989. Characterization of a monoclonal antibody which detects all murine αβ T cell receptors. J. Immunol. 142:2736.
38. Khilko, S. N., M. Corr, L. F. Boyd, A. Lees, J. K. Inman, and D. H. Margulies. 1993. Direct detection of major bistocompatibility complex class I binding to antigenic peptides using surface plasmon resonance. Peptide immobilization and characterization of binding specificity. J. Biol. Chem. 268:15425.
39. Pharmacia. 1995. BIAevaluation Software Handbook, Version 2.1. Pharmacia Biosensor AB, Uppsala.
40. O'Shannessy, D. J., M. Brigham-Burke, K. K. Soneson, P. Hensley, and I. Brooks. 1993. Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: use of nonlinear least squares analysis methods. Anal. Biochem. 212:457.
41. McPhie, P., and R. I. Shrager. 1992. An investigation of the thermal unfolding of swine pepsinogen using circular dichroism. Arch. Biochem. Biophys. 293:46.
42. Provencher, S. W., and J. Glockner. 1981. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20:33.
43. Kozlowski, S., M. Corr, T. Takeshita, L. Boyd, C. Pendleton, R. Germain, J. Berzofsky, and D. H. Margulies. 1992. Serum angiotensin-1 converting enzyme activity processes a human immunodeficiency virus 1 gp160 peptide for presentation by major histocompatibility complex class I molecules. J. Exp. Med. 175:1417.
44. 2-microglobulin regulation of cell surface MHC class I conformation and expression. J. Immunol. 148:3723.
45. Bikoff, E. K., G. R. Otten, and E. J. Robertson. 1991. Defective assembly of class I major histocompatibility complex molecules in an embryonic cell line. Eur. J. Immunol. 21:1997.
46. Ozato, K., N. Mayer, and D. Sachs. 1982. Monoclonal antibodies to mouse major histocompatibility complex antigens. Transplantation 34:113.
47. Takeshita, T., H. Takahashi, S. Kozlowski, J. D. Ahlers, C. D. Pendleton, R. L. Moore, Y. Nakagawa, K. Yokomuro, B. S. Fox, D. H. Margulies, and J. A. Berzofsky. 1995. Molecular analysis of the same HIV peptide functionally binding to both a class I and a class II MHC molecule. J. Immunol. 154:1973.
48. Fields, B. A., X. Ysern, R. J. Poljak, X. Shao, E. S. Ward, and R. A. Mariuzza. 1994. Crystallization and preliminary x-ray diffraction study of a bacterially produced T-cell antigen receptor Vα domain. J. Mol. Biol. 239:339.
49. Schlueter, C. J., B. A. Schodin, S. Y. Tetin, and D. M. Kranz. 1996. Specificity and binding properties of a single-chain T cell receptor. J. Mol. Biol. 256:859.
50. HER2 antibody Fab fragments. Biochemistry 31:5434.
51. Lilie, H., R. Rudolph, and J. Buchner. 1995. Association of antibody chains at different stages of folding: prolyl isomerization occurs after formation of quaternary structure. J. Mol. Biol. 248:190.
52. Lilie, H., R. Jaenicke, and J. Buchner. 1995. Characterization of a quaternary-structured folding intermediate of an antibody Fab-fragment. Protein Sci. 4:917.
53. Lilie, H., and J. Buchner. 1995. Domain interactions stabilize the alternatively folded state of an antibody Fab fragment. FEBS Lett. 362:43.
54. Jönsson, U., L. Fägerstam, B. Ivarsson, B. Johnsson, R. Karlsson, K. Lundh, S. Löfås, B. Persson, H. Roos, I. Rönnberg, S. Golander, R. Stahlberg, E. Sternberg, and C. Urbaniczky. 1991, Real-time biospecific interaction analysis using surface plasmon resonance and a sensor chip technology. Biotechniques 11:620.
55. Khilko, S. N., M. T. Jelonek, M. Corr, L. F. Boyd, A. L. M. Bothwell, and D. H. Margulies. 1995. Measuring interactions of MHC class I molecules using surface plasmon resonance. J. Immunol. Methods 183:77.
56. Lyons, D. S., S. A. Lieberman, J. Hampl, J. J. Boniface, Y.-H. Chien, L. J. Berg, and M. M. Davis. 1996. A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists. Immunity 5:53.
57. Matsui, K., J. J. Boniface, P. Steffner, P. A. Reay, and M. M. Davis. 1994. Kinetics of T-cell receptor binding to peptide/I-Ek complexes: correlation of the dissociation rate with T-cell responsiveness. Proc. Natl. Acad. Sci. USA 91:12862.
58. Scott, C. A., K. C. Garcia, F. R. Carbone, I. A. Wilson, and L. Teyton. 1996. Role of chain pairing for the production of functional soluble IA major histocompatibility complex class II molecules. J. Exp. Med. 183:2087.
59. Reiter, Y., I. Kurucz, U. Brinkmann, S. H. Jung, B. Lee, D. M. Segal, and I. Pastan. 1995. Construction of a functional disulfide-stabilized TCR Fv indicates that antibody and TCR Fv frameworks are very similar in structure. Immunity 2:281.
60. Bikoff, E. K., L. Jaffe, R. K. Ribaudo, G. R. Otten, R. N. Germain, and E. J. Robertson. 1991. MHC class I surface expression in embryo-derived cell lines inducible with peptide or interferon. Nature 354:235.
61. Yanagi, Y., Y. Yoshikai, K. Leggett, S. P. Clark, I. Aleksander, and T. W. Mak. 1984. A human T cell-specific cDNA clone encodes a protein having extensive homology to immunoglobulin chains. Nature 308:145.
62. Hedrick, S. M., D. I. Cohen, E. A. Nielsen, and M. M. Davis. 1984. Isolation of cDNA clones encoding T cell-specific membrane-associated proteins. Nature 308:149.
63. Sykulev, Y., A. Brunmark, M. Jackson, R. J. Cohen, P. A. Peterson, and H. N. Eisen. 1994. Kinetics and affinity of reactions between an antigen-specific T cell receptor and peptide-MHC complexes. Immunity 1:15.
64. Kurucz, I., J. A. Titus, C. R. Jost, and D. M. Segal. 1995. Correct disulfide paring and efficient refolding of detergent-solublized single-chain Fv proteins from bacterial inclusion bodies. Mol. Immunol. 32:1443.
65. Matsui, K., 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.
66. Sykulev, Y., R. J. Cohen, and H. N. Eisen. 1995. The law of mass action governs antigen-stimulated cytolytic activity of CD8(+) cytotoxic T lymphocytes. Proc. Natl. Acad. Sci. USA 92:11990.
67. Al-Ramadi, B. K., M. T. Jelonek, L. F. Boyd, D. H. Margulies, and A. L. M. Bothwell. 1995. Lack of strict correlation of functional sensitization with the apparent affinity of MHC/peptide complexes for the T cell receptor. J. Immunol. 155:662.
68. + cytotoxic T lymphocytes by peptide and purified cell-free class I molecules. Int. Immunol. 5:1129.
69. Kurata, A., and J. A. Berzofsky. 1990. Analysis of peptide residues interacting with MHC molecule or T cell receptor: Can a peptide bind in more than one way to the same MHC molecule? J. Immunol. 144:4526.
70. Fields, B. A., B. Ober, E. L. Malchiodi, M. I. Lebedeva, B. C. Braden, X. Ysern, 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.
71. Duc, H. T., P. Rucay, S. Righenzi, O. Halle-Pannenko, and P. Kourilsky. 1993. Monoclonal antibodies directed against T cell epitopes presented by class I MHC antigens. Int. Immunol. 5:427.
72. Andersen, P. S., A. Stryhn, B. E. Hansen, L. Fugger, J. Engberg, and S. Buus. 1996. A recombinant antibody with the antigen-specific, major histocompatibility complex-restricted specificity of T cells. Proc. Natl. Acad. Sci. USA 93:1820.
73. Eastman, S., M. Deftos, P. C. DeRoos, D. H. Hsu, L. Teyton, N. S. Braunstein, C. J. Hackett, and A. Rudensky. 1996. A study of complexes of class II invariant chain peptide: major histocompatibility complex class II molecules using a new complex-specific monoclonal antibody. Eur. J. Immunol. 26:385.