The Surface Glycoproteins of Trypanosoma cruzi Encode a Superfamily of Variant T Cell Epitopes

Journal of Immunology

Volumn 159, Issue 9, 1997, Pages 4444-4451

  Kahn, Stuart J ^a   Wleklinski, Monika ^a  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; MEMBRANE PROTEIN; PARASITE ANTIGEN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; C57BL MOUSE; CELL LINE; FEMALE; GENETICS; IMMUNOLOGY; MOLECULAR GENETICS; MOUSE; TRYPANOSOMA CRUZI;

AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, PROTOZOAN; CELL LINE; EPITOPES, T-LYMPHOCYTE; FEMALE; MEMBRANE GLYCOPROTEINS; MICE; MICE, INBRED C57BL; MOLECULAR SEQUENCE DATA; TRYPANOSOMA CRUZI;

EID: 0031278587     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (58)

1. WHO. 1991. Control of Chagas' disease. In WHO Technical Report Series 811. World Health Organization, Geneva, p. 95.
2. +) T lymphocytes. Infect. Immun. 57:2246.
3. Tarleton, R. L., B. H. Koller, A. Latour, and M. Postan. 1992. Susceptibility of beta 2-microglobulin-deficient mice to Trypanosoma cruzi infection. Nature 356: 338.
4. + T-cell subsets in vivo. Immunol. Rev. 123:189.
5. Hoft, D. F., R. G. Lynch, and L. V. Kirchhoff. 1993. Kinetic analysis of antigen-specific immune responses in resistant and susceptible mice during infection with Trypanosoma cruzi. J. Immunol. 151:7038.
6. Zhang, L., and R. L. Tarleton. 1996. Characterization of cytokine production in murine Trypanosoma cruzi infection by in situ immunocytochemistry: lack of association between susceptibility and type 2 cytokine production. Eur. J. Immunol. 26:102.
7. Silva, J. S., P. J. Morrissey, K. H. Grabstein, K. M. Mohler, D. Anderson, and S. G. Reed. 1992. Interleukin 10 and interferon gamma regulation of experimental Trypanosoma cruzi infection. J. Exp. Med. 175:169.
8. Silva, J. S., D. R. Twardzik, and S. G. Reed. 1991. Regulation of Trypanosoma cruzi infections in vitro and in vivo by transforming growth factor beta (TGF-beta). J. Exp. Med. 174:539.
9. Reed, S. G., J. A. Inverso, and S. B. Roters. 1984. Suppressed antibody responses to sheep erythrocytes in mice with chronic Trypanosoma cruzi infections are restored with interleukin 2. J. Immunol. 133:3333.
10. Choromanski, L., and R. E. Kuhn. 1985. Interleukin 2 enhances specific and nonspecific immune responses in experimental Chagas' disease. Infect. Immun. 50:354.
11. Reed, S. G. 1988. In vivo administration of recombinant IFN-γ induces macrophage activation, and prevents acute disease, immune suppression, and death in experimental Trypanosoma cruzi infections. J. Immunol. 140:4342.
12. Demotz, S., H. M. Grey, and A. Sette. 1990. The minimal number of class II MHC-antigen complexes needed for T cell activation. Science 249:1028.
13. Harding, C. V., and E. R. Unanue. 1990. Quantitation of antigen-presenting cell MHC class II/peptide complexes necessary for T-cell stimulation. Nature 346: 574.
14. Viola, A., and A. Lanzavecchia. 1996. T cell activation determined by T cell receptor number and tunable thresholds. Science 273:104.
15. Evavold, B. D., J. Sloan-Lancaster, and P. M. Allen. 1993. Tickling the TCR: selective T-cell functions stimulated by altered peptide ligands. Immunol. Today 14:602.
16. Evavold, B. D., J. Sloan-Lancaster, B. L. Hsu, and P. M. Allen. 1993. Separation of T helper 1 clone cytolysis from proliferation and lymphokine production using analog peptides. J. Immunol. 150:3131.
17. Pfeiffer, C., J. Stein, S. Southwood, H. Ketelaar, A. Sette, and K. Bottomly. 1995. Altered peptide ligands can control CD4 T lymphocyte differentiation in vivo. J. Exp. Med. 181:1569.
18. Nicholson, L. B., J. M. Greer, R. A. Sobel, M. B. Lees, and V. K. Kuchroo. 1995. An altered peptide ligand mediates immune deviation and prevents autoimmune encephalomyelitis. Immunity 3:397.
19. Kumar, V., V. Bhardwaj, L. Soares, J. Alexander, A. Sette, and E. Sercarz. 1995. Major histocompatibility complex binding affinity of an antigenic determinant is crucial for the differential secretion of interleukin 4/5 or interferon gamma by T cells. Proc. Natl. Acad. Sci. USA 92:9510.
20. Sloan-Lancaster, J., and P. Allen. 1996. Altered peptide ligand-induced partial t cell activation: molecular mechanisms and role in T cell biology. Annu. Rev. Immunol. 14:1.
21. Chaturvedi, P., Q. Yu, S. Southwood, A. Sette, and B. Singh. 1996. Peptide analogs with different affinities for MHC alter the cytokine profile for of T helper cells. Int. Immunol. 8:745.
22. Campetella, O., D. Sanchez, J. J. Cazzulo, and A. C. C. Frasch. 1992. A Superfamily of Trypanosoma cruzi surface antigens. Parasitol. Today 8:378.
23. Kahn, S., W. C. Van Voorhis, and H. Eisen. 1990. The major 85-kD surface antigen of the mammalian form of Trypanosoma cruzi is encoded by a large heterogeneous family of simultaneously expressed genes. J. Exp. Med. 172:589.
24. Van Voorhis, W. C., L. Barrett, R. Koelling, and A. G. Farr. 1993. FL-160 proteins of Trypanosoma cruzi are expressed from a multigene family and contain two distinct epitopes that mimic nervous tissues. J. Exp. Med. 178:681.
25. Kahn, S., T. G. Colbert, J. C. Wallace, N. A. Hoagland, and H. Eisen. 1991. The major 85-kDa surface antigen of the mammalian-stage forms of Trypanosoma cruzi is a family of sialidases. Proc. Natl. Acad. Sci. USA 88:4481.
26. Kahn, S., M. Kahn, W. C. Van Voorhis, A. Goshorn, A. Strand, N. Hoagland, H. Eisen, and S. Pennathur. 1993. SA85-1 proteins of Trypanosoma cruzi lack sialidase activity. Mol. Biochem. Parasitol. 60:149.
27. Ouaissi, M. A., J. Cornette, and A. Capron. 1986. Identification and isolation of Trypanosoma cruzi trypomastigote cell surface protein with properties expected of a fibronectin receptor. Mol. Biochem. Parasitol. 19:201.
28. Boschetti, M. A., M. M. Piras, D. Henriquez, and R. Piras. 1987. The interaction of a Trypanosama cruzi surface protein with Vero cells and its relationship with parasite adhesion. Mol. Biochem. Parasitol. 24:175.
29. Abuin, G., W. Colli, W. de Souza, and M. J. Alves. 1989. A surface antigen of Trypanosoma cruzi involved in cell invasion (Tc-85) is heterogeneous in expression and molecular constitution. Mol. Biochem. Parasitol. 35:229.
30. Lima, M. F., and F. Villalta. 1989. Trypanosoma cruzi trypomastigote clones differentially express a parasite cell adhesion molecule. Mol. Biochem. Parasitol. 33:159.
31. Yoshida, N., S.A. Blanco, M. F. Araguth, M. Russo, and J. Gonzalez. 1990. The stage-specific 90-kilodalton surface antigen of metacyclic trypomastigotes of Trypanosoma cruzi. Mol. Biochem. Parasitol. 39:39.
32. Giordano, R., R. Chammas, S. S. Veiga, W. Colli, and M. J. Alves. 1994. An acidic component of the heterogeneous Tc-85 protein family from the surface of Trypanosoma cruzi is a laminin binding glycoprotein. Mol. Biochem. Parasitol. 65:85.
33. Schenkman, S., D. Eichinger, M. E. Pereira, and V. Nussenzweig. 1994. Structural and functional properties of Trypanosoma trans-sialidase. Annu. Rev. Microbiol. 48:499.
34. Kahn, S., M. Wleklinski, A. Aruffo, A. Farr, D. Coder, and M. Kahn. 1995. Trypanosoma cruzi amastigote adhesion to macrophages is facilitated by the mannose receptor. J. Exp. Med. 182:1243.
35. Kahn, S. J., M. Wleklinski, R. A. B. Ezekowitz, D. Coder, A. Aruffo, and A. Farr. 1996. The major surface glycoproteins of Trypanosoma cruzi amastigotes are ligands of the human serum mannose binding protein. Infect. Immun. 64:2649.
36. Plata, F., F. Garcia-Pons, and H. Eisen. 1984. Antigenic polymorphism of Trypanosoma cruzi: clonal analysis of trypomastigote surface antigens. Eur. J. Immunol. 14:392.
37. Rosenberg, A. H., B. N. Lade, D. S. Chui, S. W. Lin, J. J. Dunn, and F. W. Studier. 1987. Vectors for selective expression of cloned DNAs by T7 RNA polymerase. Gene 56:125.
38. Kroll, D. J., H. Abdel-Malek-Abdel-Hafiz, T. Marcell, S. Simpson, C. Y. Chen, H.-A. Gutierrez, J. W. Lustbader, and J. P. Hoeffler. 1993. A multifunctional prokaryotic protein expression system: overproduction, affinity purification, and selective detection. DNA Cell Biol. 12:441.
39. Kruisbeek, A. M. 1992. Production of mouse T cell hybridomas. In Current Protocols in Immunology. J. E. Coligan, A. M. Kruisbeek, D. Margulies, E. Shevach, and W. Strober, eds. Green Publishing and Wiley-Interscience, New York, p. 3.14.1.
40. Fitch, F. W., and T. F. Gajewski. 1992. Production of mouse T cell clones. In Current Protocols in Immunology. J. E. Coligan, A. M. Kruisbeek, D. Margulies, E. Shevach, and W. Strober, eds. Green Publishing and Wiley-Interscience, New York, p. 3.13.1.
41. Bhattacharya, A., M. E. Dorf, and T. A. Springer. 1981. A shared alloantigenic determinant on Ia antigens encoded by the I-A and I-E subregions: evidence for I region gene duplication. J. Immunol. 127:2488.
42. Davis, L., P. Lipsky, and K. Bottomly. 1995. Measurement of human and murine interleukin 2 and interleukin 4. In Current Protocols in Immunology. J. E. Coligan, A. M. Kruisbeek, D. Margulies, E. Shevach, and W. Strober, eds. Green Publishing and Wiley-Interscience, New York, p. 6.3.1.
43. 3H]thymidine incorporation assay. J. Immunol. Methods 170: 211.
44. Kruisbeek, A. M., and E. Shevach. 1991. Proliferative assays for T cell function. In Current Protocols in Immunology. J. E. Coligan, A. M. Kruisbeek, D. Margulies, E. Shevach, and W. Strober, eds. Green Publishing and Wiley-Interscience, New York, p. 3.12.1.
45. Coffman, R. L., and I. L. Weissman. 1981. B220: a B cell-specific member of the T200 glycoprotein family. Nature 289:681.
46. Ledbetter, J. A., and L. A. Herzenberg. 1979. Xenogeneic monoclonal antibodies to mouse lymphoid differentiation antigens. Immunol. Rev. 47:63.
47. Sarmiento, M., M. R. Loken, and F. W. Fitch. 1981. Structural differences in cell surface T25 polypeptides from thymocytes and cloned T cells. Hybridoma 1:13.
48. Ceredig, R., J. W. Lowenthal, M. Nabholz, and H. R. MacDonald. 1985. Expression of interleukin-2 receptors as a differentiation marker on intrathymic stem cells. Nature 314:98.
49. + T cells during initiation of infection. J. Exp. Med. 179:447.
50. Van Voorhis, W. C., and H. Eisen. 1989. FI-160: a surface antigen of Trypanosoma cruzi that mimics mammalian nervous tissue. J. Exp. Med. 169:641.
51. Andrews, N. W., K. S. Hong, E. S. Robbins, and V. Nussenzweig. 1987. Stage-specific surface antigens expressed during the morphogenesis of vertebrate forms of Trypanosoma cruzi. Exp. Parasitol. 64:474.
52. Ley, V., N. W. Andrews, E. S. Robbins, and V. Nussenzweig. 1988. Amastigotes of Trypanosoma cruzi sustain an infective cycle in mammalian cells. J. Exp. Med. 168:649.
53. + T cells. J. Exp. Med. 182:1591.
54. + T helper cell phenotype development in a T cell receptor-alpha beta-transgenic model. J. Exp. Med. 182:1579.
55. Vignali, D. A., 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.
56. + T cells in response to antagonist ligands. J. Exp. Med. 184:149.
57. Klenerman, P., S. Rowland-Jones, S. McAdam, J. Edwards, S. Daenke, D. Lalloo, B. Koppe, W. Rosenberg, D. Boyd, A. Edwards, P. Giangrande, R. E. Phillips, and A. J. McMichael. 1994. Cytotoxic T-cell activity antagonized by naturally occurring HIV-1 Gag variants. Nature 369:403.
58. Bertoletti, A., A. Sette, F. V. Chisari, A. Penna, M. Levrero, M. de Carli, F. Fiaccadori, and C. Ferrari. 1994. Natural variants of cytotoxic epitopes are T-cell receptor antagonists for antiviral cytotoxic T cells. Nature 369:407.