Post-translational modifications of naturally processed MHC-binding epitopes

被引:94
作者
Engelhard, VH [1 ]
Altrich-Vanlith, M
Ostankovitch, M
Zarling, AL
机构
[1] Univ Virginia, Sch Med, Carter Ctr Immunol Res, Charlottesville, VA 22908 USA
[2] Univ Virginia, Sch Med, Dept Microbiol, Charlottesville, VA 22908 USA
关键词
D O I
10.1016/j.coi.2005.11.015
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
A variety of different post-translational modifications of peptides displayed by class I and II MHC molecules have now been described. Some modifications promote the binding of peptides to MHC molecules, and might also influence the ability of the peptide to be produced by antigen processing pathways. In some instances, the antigen processing components themselves are actually responsible for generating post-translational modifications. Finally, evidence is accumulating that modifications can be altered as a consequence of inflammation, transformation, apoptosis and aging. This leads to altered repertories of MHC-associated peptides, which may be important in immune responses associated with autoimmune diseases, infection and cancer.
引用
收藏
页码:92 / 97
页数:6
相关论文
共 55 条
[31]   T cell recognition and therapeutic effect of a phosphorylated synthetic peptide of the 70K snRNP protein administered in MRL/Ipr mice [J].
Monneaux, F ;
Lozano, JM ;
Patarroyo, ME ;
Briand, JP ;
Muller, S .
EUROPEAN JOURNAL OF IMMUNOLOGY, 2003, 33 (02) :287-296
[32]   Asparagine deamidation perturbs antigen presentation on class II major histocompatibility complex molecules [J].
Moss, CX ;
Matthews, SP ;
Lamont, DJ ;
Watts, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (18) :18498-18503
[33]   Tyrosinase degradation via two pathways during reverse translocation to the cytosol [J].
Mosse, CA ;
Hsu, W ;
Engelhard, VH .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2001, 285 (02) :313-319
[34]  
Neugebauer KM, 2000, ARTHRITIS RHEUM, V43, P1768, DOI 10.1002/1529-0131(200008)43:8<1768::AID-ANR13>3.0.CO
[35]  
2-9
[36]   Immunogenicity of an inflammation-associated product, tyrosine nitrated self-proteins [J].
Ohmori, H ;
Kanayama, N .
AUTOIMMUNITY REVIEWS, 2005, 4 (04) :224-229
[37]   Tissue transglutaminase: apoptosis versus autoimmunity [J].
Piacentini, M ;
Colizzi, V .
IMMUNOLOGY TODAY, 1999, 20 (03) :130-134
[38]  
Pierce RA, 1999, J IMMUNOL, V163, P6360
[39]   Refining the rules of gliadin T cell epitope binding to the disease-associated DQ2 molecule in celiac disease: Importance of proline spacing and glutamine deamidation [J].
Qiao, SW ;
Bergseng, E ;
Molberg, O ;
Jung, G ;
Fleckenstein, B ;
Sollid, LM .
JOURNAL OF IMMUNOLOGY, 2005, 175 (01) :254-261
[40]   Antigen presentation to celiac lesion-derived T cells of a 33-mer gliadin peptide naturally formed by gastrointestinal digestion [J].
Qiao, SW ;
Bergseng, E ;
Molberg, O ;
Xia, J ;
Fleckenstein, B ;
Khosla, C ;
Sollid, LM .
JOURNAL OF IMMUNOLOGY, 2004, 173 (03) :1757-1762