Frequent occurrence of anti-tRNA(His) autoantibodies that recognize a conformational epitope in sera of patients with myositis

Arthritis and Rheumatism

Volumn 41, Issue 8, 1998, Pages 1428-1437

  Brouwer, Rick ^a   Egberts, Wilma Vree ^a   Jongen, Peter H ^b   Van Engelen, Baziel G M ^b   Van Venrooij, Walther J ^a,b  

^a RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

^b RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; RNA ANTIBODY; TRANSFER RNA;

ANTIBODY DETECTION; ANTIBODY SPECIFICITY; ARTICLE; HUMAN; HUMAN CELL; MAJOR CLINICAL STUDY; MOLECULAR INTERACTION; MYOSITIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; RNA SEQUENCE;

AUTOANTIBODIES; CROSS REACTIONS; EPITOPES; HISTIDINE-TRNA LIGASE; HUMANS; MOLECULAR CONFORMATION; MYOSITIS; PEPTIDE FRAGMENTS; PRECIPITIN TESTS; RNA; RNA, TRANSFER, HIS;

EID: 0031826939     PISSN: 00043591     EISSN: None     Source Type: Journal    
DOI: 10.1002/1529-0131(199808)41:8<1428::AID-ART12>3.0.CO;2-J     Document Type: Article

References (38)

1. Plotz PH, Rider LG, Targoff IN, Raben N, O'Hanlon TP, Miller FW. NIH conference. Myositis: immunologic contributions to understanding cause, pathogenesis, and therapy. Ann Intern Med 1995;122:715-24.
2. Hohlfeld R, Engel AG. The immunobiology of muscle. Immunol Today 1994;15:269-74.
3. Love LA, Leff RL, Fraser DD, Targoff IN, Dalakas M, Plotz PH, et al. A new approach to the classification of idiopathic inflammatory myopathy: myositis-specific autoantibodies define useful homogeneous patient groups. Medicine (Baltimore) 1991;70:360-74.
4. Plotz PH, Targoff IN. Myositis-associated antigens: aminoacyl-tRNA synthetases Jo-1, PL-7, PL-12, EJ, and OJ. In: van Venrooij WJ, Maini RN, editors. Manual of biological markers of disease. Dordrecht: Kluwer Academic Publishers; 1994. p. B6.1/1-B6.1/18.
5. Targoff IN. Immune manifestations of inflammatory muscle disease. Rheum Dis Clin North Am 1994;20:857-80.
6. Targoff IN, Plotz PH. The autoantibody system: anti-aminoacyl-tRNA synthetase antibodies. In: van Venrooij WJ, Maini RN, editors. Manual of biological markers. Dordrecht: Kluwer Academic Publishers; 1996. p. C6.1/1-C6.1/12.
7. Carter CWJ. Cognition, mechanism, and evolutionary relationships in aminoacyl-tRNA synthetases. Annu Rev Biochem 1993; 62:715-48.
8. Burbaum JJ, Schimmel P. Structural relationships and the classification of aminoacyl-tRNA synthetases. J Biol Chem 1991;266: 16965-8.
9. Gelpí C, Kanterewicz E, Gratacos J, Targoff IN, Rodriguez-Sanchez JL. Coexistence of two antisynthetases in a patient with the antisynthetase syndrome. Arthritis Rheum 1996;39:692-7.
10. Raben N, Nichols R, Dohlman J, McPhie P, Sridhar V, Hyde C, et al. A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope. J Biol Chem 1994;269:24277-83.
11. Miller FW, Twitty SA, Biswas T, Plotz PH. Origin and regulation of a disease-specific autoantibody response: antigenic epitopes, spectrotype stability, and isotype restriction of anti-Jo-1 autoantibodies. J Clin Invest 1990;85:468-75.
12. Martin A, Shulman MJ, Tsui FW. Epitope studies indicate that histidyl-tRNA synthetase is a stimulating antigen in idiopathic myositis. FASEB J 1995;9:1226-33.
13. Bunn CC, Bernstein RM, Mathews MB. Autoantibodies against alanyl-tRNA synthetase and tRNAAla coexist and are associated with myositis. J Exp Med 1986;163:1281-91.
14. Bunn CC, Mathews MB. Autoreactive epitope defined as the anticodon region of alanine transfer RNA. Science 1987;238: 1116-9.
15. Bohan A, Peter JB, Bowman RL, Pearson CM. Computer-assisted analysis of 153 patients with polymyositis and dermatomyositis. Medicine (Baltimore) 1977;56:255-86.
16. Rutjes SA, Vree Egberts WTM, Jongen P, van den Hoogen F, Pruijn GJM, van Venrooij WJ. Anti-Ro52 antibodies frequently co-occur with anti-Jo-1 antibodies in sera from patients with idiopathic inflammatory myopathy. Clin Exp Immunol 1997;109: 32-40.
17. Sprinzl M, Steegborn C, Hubel F, Steinberg S. Compilation of tRNA sequences and sequences of tRNA genes. Nucleic Acids Res 1996;24:68-72.
18. Ashburner M. Drosophila, a laboratory manual. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1989.
19. Rosa MD, Hendrick JPJ, Lerner MR, Steitz JA, Reichlin M. A mammalian tRNAHis-containing antigen is recognized by the polymyositis-specitic antibody anti-Jo-1. Nucleic Acids Res 1983; 11:853-70.
20. Bjork GR. Biosynthesis and function of modified nucleotides. In: Soll D, RajBhandary U, editors. tRNA: structure, biosynthesis, and function. Washington (DC): American Society for Microbiology; 1995. p. 165.
21. Holbrook SR, Sussman JL, Warrant RW, Church GM, Kim SH. RNA-ligand interactions. I. Magnesium binding sites in yeast tRNAPhe. Nucleic Acids Res 1977;4:2811-20.
22. Jack A, Ladner JE, Rhodes D, Brown RS, Klug A. A crystallographic study of metal-binding to yeast phenylalanine transfer RNA. J Mol Biol 1977;111:315-28.
23. Vázquez-Abad D, Rothfield NF. Sensitivity and specificity of anti-Jo-1 antibodies in autoimmune diseases with myositis. Arthritis Rheum 1996;39:292-6.
24. Targoff IN. Humoral immunity in polymyositis/dermatomyositis. J Invest Dermatol 1993;100:116S-23S.
25. Mathews MB, Bernstein RM. Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity. Nature 1983;304:177-9.
26. Bernstein RM, Bunn CC, Hughes GR, Francoeur AM, Mathews MB. Cellular protein and RNA antigens in autoimmune disease. Mol Biol Med 1984;2:105-20.
27. Hoet RM, Koornneef I, de Rooij DJ, van de Putte LB, van Venrooij WJ. Changes in anti-U1 RNA antibody levels correlate with disease activity in patients with systemic lupus erythematosus overlap syndrome. Arthritis Rheum 1992;35:1202-10.
28. Bootsma H, Spronk P, Derksen R, de Boer G, Wolters Dicke H, Hermans J, et al. Prevention of relapses in systemic lupus erythematosus [published erratum appears in Lancet 1995;346:516]. Lancet 1995;345:1595-9.
29. Ladner JE, Jack A, Robertus JD, Brown RS, Rhodes D, Clark BF, et al. Structure of yeast phenylalanine transfer RNA at 2.5 A resolution. Proc Natl Acad Sci U S A 1975;72:4414-8.
30. Derrick WB, Horowitz J. Probing structural differences between native and in vitro transcribed Escherichia coli valine transfer RNA: evidence for stable base modification-dependent conformers. Nucleic Acids Res 1993;21:4948-53.
31. Rosalki SB. Serum enzymes in disease of skeletal muscle. Clin Lab Med 1989;9:767-81.
32. Ehrenstein MR, Snaith ML, Isenberg DA. Idiopathic myositis: a rheumatological view. Ann Rheum Dis 1992;51:41-4.
33. Francklyn C, Schimmel P. Enzymatic aminoacylation of an eight-base-pair microhelix with histidine. Proc Natl Acad Sci U S A 1990;87:8655-9.
34. Rudinger J, Florentz C, Giege R. Histidylation by yeast HisRS of tRNA or tRNA-like structure relies on residues -1 and 73 but is dependent on the RNA context. Nucleic Acids Res 1994;22: 5031-7.
35. Nameki N, Asahara H, Shimizu M, Okada N, Himeno H. Identity elements of Saccharomyces cerevisiae tRNA(His). Nucleic Acids Res 1995;23:389-94.
36. Arnez JG, Harris DC, Mitschler A, Rees B, Francklyn CS, Moras D. Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate. EMBO J 1995;14:4143-55.
37. Miller FW, Waite KA, Biswas T, Plotz PH. The role of an autoantigen, histidyl-tRNA synthetase, in the induction and maintenance of autoimmunity. Proc Natl Acad Sci USA 1990;87: 9933-7.
38. Desai-Mehta A, Mao C, Rajagopalan S, Robinson T, Datta S. Structure and specificity of T-cell receptors expressed by potentially pathogenic anti-DNA autoantibody-inducing T-cells in human lupus. J Clin Invest 1995;95:531-41.