Human transaldolase and cross-reactive viral epitopes identified by autoantibodies of multiple sclerosis patients

Journal of Immunology

Volumn 163, Issue 7, 1999, Pages 4027-4032

  Esposito, Maria ^a   Venkatesh, Vijay ^a   Otvos, Laszlo ^b   Weng, Zhiping ^c   Vajda, Sandor ^c   Banki, Katalin ^a   Perl, Andras ^a  

^a SUNY UPSTATE MEDICAL UNIVERSITY   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c Boston University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AUTOANTIBODY; EPITOPE; TRANSALDOLASE;

ALPHA HELIX; ARTICLE; AUTOIMMUNE DISEASE; CLINICAL ARTICLE; CONTROLLED STUDY; CROSS REACTION; CRYSTAL STRUCTURE; EPSTEIN BARR VIRUS; ESCHERICHIA COLI; HERPES SIMPLEX VIRUS 1; HUMAN; HUMAN CELL; HUMAN TISSUE; MOLECULAR MIMICRY; MULTIPLE SCLEROSIS; OLIGODENDROGLIA; PRIORITY JOURNAL; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; ANTIGENS, VIRAL; AUTOANTIBODIES; AUTOANTIGENS; COMPUTER SIMULATION; CROSS REACTIONS; EPITOPES, B-LYMPHOCYTE; HUMANS; IMMUNODOMINANT EPITOPES; MODELS, MOLECULAR; MOLECULAR MIMICRY; MOLECULAR SEQUENCE DATA; MULTIPLE SCLEROSIS; PEPTIDE MAPPING; SEQUENCE HOMOLOGY, AMINO ACID; TRANSALDOLASE;

EID: 0033215425     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (46)

1. Martin, R., H. F. McFarland, and D. E. McFarlin. 1992. Immunological aspects of demyelinating diseases. Annu. Rev. Immunol. 10:153.
2. Fujinami, R. S., and M. B. Oldstone. 1985. Amino acid homology between the encephalitogenic site of myelin basic protein and virus: mechanism for autoimmunity. Science 230:1043.
3. Shaw, S. Y., R. A. Laursen, and M. B. Lees. 1986. Analogous ammo acid sequences in myelin proleolipid and viral proteins. FEBS Lett. 207:266.
4. Antel, J. P., and N. R. Cashman. 1991. Human retrovirus and multiple sclerosis. Mayo Clin. Proc. 66:752.
5. Perl, A., and K. Banki. 1993. Human endogenous retroviral elements and autoimmunity: data and concepts. Trends Microbiol. 1:153.
6. Murphy, P. M. 1993. Molecular mimicry and the generation of host defense protein diversity. Cell 72:823.
7. Steinman, L., A. Waisman, and D. Altmann. 1996. Major T cell responses in multiple sclerosis. Mol. Med. Today 1:79.
8. Banki, K., E. Colombo, F. Sia, D. Halladay, D. Mattson, A. Tatum, P. Massa, P. E. Phillips, and A. Perl. 1994. Oligodendrocyte-specific expression and autoantigenicity of transaldolase in multiple sclerosis. J. Exp. Med. 180:1649.
9. Banki, K., D. Halladay, and A. Perl. 1994. Cloning and expression of the human gene for transaldolase: a novel highly repetitive element constitutes an integral part of the coding sequence. J. Biol. Chem. 269:2847.
10. Banki, K., and A. Perl. 1996. Inhibition of the catalytic activity of human transaldolase by antibodies and site-directed mutagenesis. FEBS Lett. 378:161.
11. Colombo, E., K. Banki, A. H. Tatum, J. Daucher, P. Ferrante, R. S. Murray, P. E. Phillips, and A. Perl. 1997. Comparative analysis of antibody and cell-mediated autoimmunity to transaldolase and myetin basic protein in patients with multiple sclerosis. J. Clin. Invest. 99:1238.
12. Hotta, S. S. 1962. Glucose metabolism in brain tissue: the hexose-monophosphate shunt and its role in glutathione reduction. J. Neurochem. 9:43.
13. Mayes, P. 1993. The pentose phosphate pathway & other pathways of hexose metabolism. In Harper's Biochemistry, 23rd Ed. R. Murray, D. Granner, P. Mayes and V. Rodwell, eds. Appleton & Lange, Norwalk, p. 201.
14. Banki, K., E. Hutter, E. Colombo, N. J. Gonchoroff, and A. Perl. 1996. Glutathione levels and sensitivity to apoptosis are regulated by changes in transaldolase expression. J. Biol. Chem. 271:32994.
15. Ni, T., and M. A. Savageau. 1996. Application of biochemical systems theory to metabolism in human red blood cells: signal propagation and accuracy of representation. J. Biol. Chem. 271:7927.
16. Banki, K., R. L. Eddy, T. B. Shows, D. L. Halladay, F. Bullrich, C. M. Croce, V. Jurecic, A. Baldini, and A. Perl. 1997. The human transaldolase gene (TALDO1) is located on chromosome 11 at p15. 4 - p15.5. Genomics 45:233.
17. Haines, J. L., M. Ter-Minassian, A. Bazyk, J. F. Gusella, D. J. Kim, H. Terwedow, M. A. Pericak-Vance, J. B. Rimmler, C. S. Haynes, A. D. Roses, et al. 1996. A complete genomic screen for multiple sclerosis underscores a role for the major histocompatibility complex. Nat. Genet. 13:469.
18. Poser, C. M., D. W. Paty, L. Scheinberg, W. I. McDonald, F. A. Davis, G. C. Ebers, K. P. Johnson, W. A. Sibley, W. H. Silberberg, and W. W. Tourtellotte. 1983. New diagnostic criteria for multiple sclerosis: guidelines for research protocols. Ann. Neurol. 13:227.
19. Frank, R. 1992. SPOT synthesis: an easy technique for the positionally addressable, parallel chemical syntesis on a membrane support. Tetrahedron 48:9217.
20. Houghton, R. A., C. Pinilla, S. E. Blondelle, J. R. Appel, C. T. Dooley, and J. H. Cuervo. 1991. Generation of synthetic peptide combinatorial libraries for basic research and drug discovery. Nature 354:84.
21. Rudiger, S., L. Germeroth, J. Schneider-Mergener, and B. Bukau. 1997. Substrate-specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16:1501.
22. Jia, J., U. Schorken, Y. Lindqvist, G. A. Sprenger, and G. Schneider. 1997. Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases. Protein Sci. 6:119.
23. Sali, A., and T. L. Blundell. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779.
24. Lee, B., and F. M. Richards. 1998. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:379.
25. Fleiss, J. L. 1981. Statistical Methods for Rates and Proportions. Wiley, New York.
26. Geysen, H. M., R. H. Meloen, and S. J. Barteling. 1984. Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid. Proc. Natl. Acad. Sci. USA 81:3998.
27. Geysen, H. M. 1990. Molecular technology: peptide epitope mapping and the pin technology. Southeast Asian J. Trop. Med. Public Health 21:523.
28. Williams, R. C., Jr., R. Staud, C. C. Malone, J. Payabyab, L. Byres, and D. Underwood. 1994. Epitopes on proteinase-3 recognized by antibodies from patients with Wegener's granulomatosis. J. Immunol. 152:4722.
29. James, J. A., R. H. Scofield, and J. B. Harley. 1994. Basic amino acids predominate in the sequential autoantigenic determinants of the small nuclear 70K ribonucleoprotein. Scand. J. Immunol. 39:557.
30. Lang, E., G. Szendrei, V. M. Y. Lee, and L. J. Otvos. 1994. Spectroscopic evidence that monoclonal antibodies recognize the dominant conformation of medium-sized synthetic peptides. J. Immunol. Methods 170:103.
31. Baig, S., O. Olsson, T. Olsson, A. Love, S. Jeansson, and H. Link. 1989. Cells producing antibody to measles and herpes simplex virus in cerebrospinal fluid and blood of patients with multiple sclerosis and controls. Clin. Exp. Immunol. 78:390.
32. Sumaya, C. V., L. V. Myers, G. W. Ellison, and Y. Ench. 1985. Increased prevalence and titer of Epstein-Barr virus antibodies in patients with multiple sclerosis. Ann. Neurol. 17:371.
33. Johnson, M., and T. Valyi-Nagy. 1998. Expanding the clinicopathologic spectrum of herpes simplex encephalitis. Hum. Pathol. 29:207.
34. Moudgil, K. D., and E. E. Sercarz. 1994. The T cell repertoire against cryptic self determinants and its involvement in autoimmunity and cancer. Clin. Immunol. Immunopathol. 73:283.
35. Oldstone, M. B. A. 1987. Molecular mimicry and autoimmune disease. Cell 50:819.
36. Wucherpfennig, K. W., and J. L. Strominger. 1995. Molecular mimicry in T cell-mediated autoimmunity: viral peptides activate human T cell clones specific for myelin basic protein. Cell 80:695.
37. Garren, H., L. Steinman, and C. Lock. 1998. The specificity of the antibody response in multiple sclerosis. Ann. Neurol. 43:4.
38. Perl, A., and K. Banki. 1999. Molecular mimicry, altered apoptosis, and immunomodulation as mechanisms of viral pathogenesis in systemic lupus erythematosus. In Lupus: Molecular and Cellular Pathogenesis. G. M. Kammer and G. C. Tsokos, eds. Humana, Totowa, p. 43.
39. Genain, C. P., B. Cannella, S. L. Hauser, and C. S. Raine. 1999. Identification of autoantibodies associated with myelin damage in multiple sclerosis. Nat. Med. 5:170.
40. Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Cryst. 24:946.
41. McGeoch, D. J., M. A. Dalrymple, A. Dolan, D. McNab, L. J. Perry, and P. Taylor. 1988. Structures of herpes simplex virus type 1 genes required for replication of virus DNA. J. Virol. 62:444.
42. Schmid, A., P. Spielhofer, R. Cattaneo, K. Baczko, V. ter Meulen, and M. A. Billeter. 1992. Subacute sclerosing panencephalitis is typically characterized by alterations in the fusion protein cytoplasmic domain of the persisting measles virus. Virology 188:910.
43. Baer, R., A. T. Bankier, M. D. Biggin, P. L. Deininger, P. J. Farrell, T. J. Gibson, G. Hatfall, G. S. Hudson, S. C. Satchwell, C. Seguin, et al. 1984. DNA sequence and expression of the B95-8 Epstein-Barr virus genome. Nature 310:207.
44. McGeoch, D. J., M. A. Dalrymple, A. J. Davison, A. Dolan, M. C. Frame, D. McNab, J. E. Scott, and P. Taylor. 1988. The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J. Gen. Virol. 69:1531.
45. Starcich, B. R., B. H. Hahn, G. M. Shaw, P. D. McNeely, S. Modrow, H. Wolf, E. S. Parks, W. P. Parks, S. F. Josephs, R. C. Gallo, et al. 1986. Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS. Cell 45:637.
46. Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387.