Posttranslational modifications of self-antigens

Annals of the New York Academy of Sciences

Volumn 1050, Issue , 2005, Pages 1-9

  Doyle, Hester A ^a   Mamula, Mark J ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Antibody; Antigen processing; Autoimmunity; MHC class II; Posttranslational modifications; T cells

Indexed keywords

AUTOANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2;

ANTIGEN PRESENTATION; ANTIGEN RECOGNITION; AUTOIMMUNE DISEASE; AUTOIMMUNITY; CONFERENCE PAPER; IMMUNOLOGICAL TOLERANCE; PROTEIN PROCESSING; T LYMPHOCYTE;

EID: 23744515712     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1196/annals.1313.001     Document Type: Conference Paper

References (41)

1. WOLD, F. 1981. In vivo chemical modification of proteins (post-translational modification). Annu. Rev. Biochem. 50: 783-814.
2. DERBINSKI, J. et al. 2001. Promiscuous gene expression in medullary thymic epithelial cells mirrors the peripheral self. Nat. Immunol. 2: 1032-1039.
3. MASSON-BESSIERE, C. et al. 2001. The major synovial targets of the rheumatoid arthritis-specific antifilaggrin autoantibodies are deiminated forms of the α- and β- chains of fibrin. J. Immunol. 166: 4177-4184.
4. CORTHAY, A. et al. 1998. Epitope glycosylation plays a critical role for T cell recognition of type II collagen in collagen-induced arthritis. Eur. J. Immunol. 28: 2580-2590.
5. CAO, L., D. SUN & J.N. WHITAKER. 1998. Citrullinated myelin basic protein induces experimental autoimmune encephalomyelitis in Lewis rats through a diverse T cell repertoire. J. Neuroimmunol. 88: 21-29.
6. ZAMVIL, S.S. et al. 1986. T-cell epitope of the autoantigen myelin basic protein that induces encephalomyelitis. Nature 324: 258-260.
7. GIRBAL-NEUHAUSER, E. et al. 1999. The epitopes targeted by the rheumatoid arthritis-associated antifilaggrin autoantibodies are posttranslationally generated on various sites of (pro)filaggrin by deimination of arginine residues. J. Immunol. 162: 585-594.
8. MYERS, L.K. et al. 2004. Relevance of posttranslational modifications for the arthritogenicity of type II collagen. J. Immunol. 172: 2970-2975.
9. MOSCARELLA, M.A. et al. 1994. Myelin in multiple sclerosis is developmentally immature. J. Clin. Invest. 94: 146-154.
10. MARTIN, R. et al. 1994. Citrulline-containing myelin basic protein is recognized by T-cell lines derived from multiple sclerosis patients and healthy individuals. Neurology 44: 123-129.
11. TRANQUIL, L.R. et al. 2000. Enhanced T cell responsiveness to citrulline-containing myelin basic protein in multiple sclerosis patients. Mult. Scler. 6: 220-225.
12. MAMULA, M.J. et al. 1999. Isoaspartyl post-translational modification triggers autoimmune responses to self-proteins. J. Biol. Chem. 274: 22321-22327.
13. YOUNG, A.L. et al. 2001. Structural integrity of histone H2B in vivo requires the activity of protein L-isoaspartate O-methyltransferase, a putitive protein repair enzyme. J. Biol. Chem. 276: 37161-37165.
14. BRAHMS, H. et al. 2000. The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies. J. Biol. Chem. 275: 17122-17129.
15. NEUGEBAUER, K.M. et al. 2000. SR proteins are autoantigens in patients with systemic lupus erythematosus: importance of phosphoepitopes. Arthritis Rheum. 43: 1768-1778.
16. HAAN, E.C. et al. 2005. Limited plasticity in T cell recognition of modified T cell receptor contact residues in MHC class II bound peptides. Mol. Immunol. 42: 355-364.
17. OTT, P.A. et al. 2004. T cells recognize multiple GAD65 and proinsulin epitopes in human type 1 diabetes, suggesting determinant spreading. J. Clin. Immunol. 24: 327-339.
18. MONNEAUX, F. & S. MULLER. 2002. Epitope spreading in systemic lupus erythematosus: identification of triggering peptide sequences. Arthritis Rheum. 46: 1430-1438.
19. LEHMANN, P.V. et al. 1992. Spreading of T cell autoimmunity to cryptic determinants of an autoantigen. Nature (Lond.) 358: 155-157.
20. 2+-free calmodulin and calmodulin damaged by in vitro aging are selectively degraded by 26 S proteasome without ubiquitination. J. Biol. Chem. 275: 20295-20301.
21. TAKEMOTO, L.J. 1995. Degradation of aspartyl and asparaginyl residues of lens proteins in vivo. In Deamidation and Isoaspartate Formation in Peptides and Proteins. D.W. Aswad, Ed.: 157-165. CRC Press. Boca Raton, FL.
22. VAN STIPDONK, M.J.B. et al. 1998. T cells discriminate between differentially phosphorylated forms of B-crystallin, a major central nervous system myelin antigen. Int. Immunol. 10: 943-950.
23. RATHMELL, J.C. & C.B. THOMPSON. 1999. The central effectors of cell death in the immune system. Annu. Rev. Immunol. 17: 781-828.
24. HERSHKO, A. & A. CIECHANOVER. 1998. The ubiquitin system. Annu. Rev. Biochem. 67: 425-479.
25. PIACENTINI, M. & V. COLIZZI. 1999. Tissue transglutaminase: apoptosis versus autoimmunity. Immunol. Today 20: 130-134.
26. ASAGA, H., M. YAMADA & T. SENSHU. 1998. Selective deimination of vimentin in calcium ionophore-induced apoptosis of mouse peritoneal macrophages. Biochem. Biophys. Res. Commun. 243: 641-646.
27. KADL, A. et al. 2004. Apoptotic cells as sources for biologically active oxidized phospholipids. Antioxid. Redox. Signal. 6: 311-20.
28. CASCIOLA-ROSEN, L.A., G. ANHALT & A. ROSEN. 1994. Autoantigens targeted in systemic lupus erythematosus are clustered in two populations of surface structures on apoptotic keratinocytes. J. Exp. Med. 179: 1317-1330.
29. UTZ, P.J. et al. 1997. Proteins phosphorylated during stress-induced apoptosis are common targets for autoantibody production in patients with systemic lupus erythematosus. J. Exp. Med. 185: 843-854.
30. PRICE, B.E. et al. 1996. Anti-phospholipid autoantibodies bind to apoptotic, but not viable, thymocytes in a beta 2-mglycoprotein I-dependent manner. J. Immunol. 157: 2201-2208.
31. LEVINE, J.S. et al. 1999. Apoptotic cells as immunogen and antigen in the antiphospholipid syndrome. Exp. Mol. Pathol. 66: 82-98.
32. CHANG, M. et al. 2004. Apoptotic cells with oxidation-specific epitopes are immunogenic and proinflammatory. J. Exp. Med. 200: 1359-1370.
33. PRITZKER, L.B. et al. 2000. Deimination of myelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D. Biochemistry 39: 5374-5381.
34. JOHNSON, B.A. & D.W. ASWAD. 1990. Fragmentation of isoaspartyl peptides and proteins by carboxypeptidase Y: release of isoaspartyl dipeptides as a result of internal and external cleavage. Biochemistry 29: 4373-4380.
35. MANOURY, B. et al. 2002. Destructive processing by asparagine endopeptidase limits presentation of a dominant T cell epitope in MBP. Nat. Immunol. 3: 169-174.
36. HILL, J.A. et al. 2003. Cutting edge: the conversion of arginine to citrulline allows for a high-affinity peptide interaction with the rheumatoid arthritis-associated HLA-DRB1*0401 MHC class II molecule. J. Immunol. 171: 538-541.
37. NIJENHUIS, S. et al. 2004. Autoantibodies to citrullinated proteins in rheumatoid arthritis: clinical performance and biochemical aspects of an RA-specific marker. Clin. Chim. Acta 350: 17-34.
38. ZENDMAN, A.J., E.R. VOSSENAAR & W.J. VAN VENROOIJ. 2004. Autoantibodies to citrullinated (poly)peptides: a key diagnostic and prognostic marker for rheumatoid arthritis. Autoimmunity 37: 295-299.
39. LOUIS, J.S. et al. 2001. Tolerance induction by acylated peptides: suppression of EAE in the mouse with palmitoylated PLP peptides. J. Neuroimmunol. 115: 79-90.
40. GREEK, J.M. et al. 2001. Thiopalmitoylation of myelin proteolipid protein epitopes enhances immunogenicity and encephalitogenicity. J. Immunol. 166: 6907-6913.
41. MONNEAUX, F. et al. 2003. T cell recognition and therapeutic effect of a phosphorylated synthetic peptide of the 70K snRNP protein administered in MR/lpr mice. Eur. J. Immunol. 33: 287-296.