Mechanisms of peptide repertoire selection by HLA-DM

Trends in Immunology

Volumn 34, Issue 10, 2013, Pages 495-501

  Pos, Wouter ^a   Sethi, Dhruv K ^a   Wucherpfennig, Kai W ^a,b  

^a DANA FARBER CANCER INSTITUTE   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

Antigen presentation; MHC class II molecules

Indexed keywords

HLA DM ANTIGEN; HLA DO ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2;

AUTOIMMUNITY; CRYSTAL STRUCTURE; NONHUMAN; PATHOGENESIS; PROTEIN BINDING; REVIEW;

ANTIGEN PRESENTATION; MHC CLASS II MOLECULES;

ANIMALS; ANTIGEN PRESENTATION; HISTOCOMPATIBILITY ANTIGENS CLASS II; HLA-D ANTIGENS; HUMANS; PEPTIDES; PROTEIN BINDING;

EID: 84883684287     PISSN: 14714906     EISSN: 14714981     Source Type: Journal    
DOI: 10.1016/j.it.2013.06.002     Document Type: Review

References (34)

1. Jenkins M.K., Moon J.J. The role of naive T cell precursor frequency and recruitment in dictating immune response magnitude. J. Immunol. 2012, 188:4135-4140.
2. Stern L.J., et al. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 1994, 368:215-221.
3. Blum J.S., et al. Pathways of antigen processing. Annu. Rev. Immunol. 2013, 31:443-473.
4. Schulze M.S., Wucherpfennig K.W. The mechanism of HLA-DM induced peptide exchange in the MHC class II antigen presentation pathway. Curr. Opin. Immunol. 2012, 24:105-111.
5. Busch R., et al. Achieving stability through editing and chaperoning: regulation of MHC class II peptide binding and expression. Immunol. Rev. 2005, 207:242-260.
6. Pashine A., et al. Interaction of HLA-DR with an acidic face of HLA-DM disrupts sequence-dependent interactions with peptides. Immunity 2003, 19:183-192.
7. Morris P., et al. An essential role for HLA-DM in antigen presentation by class II major histocompatibility molecules. Nature 1994, 368:551-554.
8. Patil N.S., et al. Rheumatoid arthritis (RA)-associated HLA-DR alleles form less stable complexes with class II-associated invariant chain peptide than non-RA-associated HLA-DR alleles. J. Immunol. 2001, 167:7157-7168.
9. Kropshofer H., et al. HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH. Immunity 1997, 6:293-302.
10. Sant A.J., et al. The relationship between immunodominance, DM editing, and the kinetic stability of MHC class II:peptide complexes. Immunol. Rev. 2005, 207:261-278.
11. Busch R., et al. On the perils of poor editing: regulation of peptide loading by HLA-DQ and H2-A molecules associated with celiac disease and type 1 diabetes. Expert Rev. Mol. Med. 2012, 14:e15.
12. Lovitch S.B., et al. Cutting edge: H-2DM is responsible for the large differences in presentation among peptides selected by I-Ak during antigen processing. J. Immunol. 2003, 171:2183-2186.
13. Doebele C.R., et al. Determination of the HLA-DM interaction site on HLA-DR molecules. Immunity 2000, 13:517-527.
14. Anders A.K., et al. HLA-DM captures partially empty HLA-DR molecules for catalyzed removal of peptide. Nat. Immunol. 2011, 12:54-61.
15. Weber D.A., et al. Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM. Science 1996, 274:618-620.
16. Sadegh-Nasseri S., et al. How HLA-DM works: recognition of MHC II conformational heterogeneity. Front. Biosci. (Schol. Ed.) 2012, 4:1325-1332.
17. Pos W., et al. Crystal structure of the HLA-DM-HLA-DR1 complex defines mechanisms for rapid peptide selection. Cell 2012, 151:1557-1568.
18. Weber D.A., et al. Transmembrane domain-mediated colocalization of HLA-DM and HLA-DR is required for optimal HLA-DM catalytic activity. J. Immunol. 2001, 167:5167-5174.
19. Zhou Z., et al. Cutting edge: HLA-DM functions through a mechanism that does not require specific conserved hydrogen bonds in class II MHC-peptide complexes. J. Immunol. 2009, 183:4187-4191.
20. Denzin L.K., Cresswell P. Sibling rivalry: competition between MHC class II family members inhibits immunity. Nat. Struct. Mol. Biol. 2013, 20:7-10.
21. Draghi N.A., Denzin L.K. H2-O, a MHC class II-like protein, sets a threshold for B-cell entry into germinal centers. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:16607-16612.
22. van den Hoorn T., et al. Routes to manipulate MHC class II antigen presentation. Curr. Opin. Immunol. 2011, 23:88-95.
23. Yi W., et al. Targeted regulation of self-peptide presentation prevents type I diabetes in mice without disrupting general immunocompetence. J. Clin. Invest. 2010, 120:1324-1336.
24. Gu Y., et al. Immunodeficiency and autoimmunity in H2-O-deficient mice. J. Immunol. 2013, 190:126-137.
25. Guce A.I., et al. HLA-DO acts as a substrate mimic to inhibit HLA-DM by a competitive mechanism. Nat. Struct. Mol. Biol. 2013, 20:90-98.
26. Yoon T., et al. Mapping the HLA-DO/HLA-DM complex by FRET and mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:11276-11281.
27. Dong G., et al. Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity 2009, 30:21-32.
28. Mage M.G., et al. The peptide-receptive transition state of MHC class I molecules: insight from structure and molecular dynamics. J. Immunol. 2012, 189:1391-1399.
29. Fallang L.E., et al. Complexes of two cohorts of CLIP peptides and HLA-DQ2 of the autoimmune DR3-DQ2 haplotype are poor substrates for HLA-DM. J. Immunol. 2008, 181:5451-5461.
30. Hou T., et al. An insertion mutant in DQA1*0501 restores susceptibility to HLA-DM: implications for disease associations. J. Immunol. 2011, 187:2442-2452.
31. Mohan J.F., Unanue E.R. A novel pathway of presentation by class II-MHC molecules involving peptides or denatured proteins important in autoimmunity. Mol. Immunol. 2013, 55:166-168.
32. Stadinski B.D., et al. Diabetogenic T cells recognize insulin bound to IAg7 in an unexpected, weakly binding register. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:10978-10983.
33. Mohan J.F., et al. Register shifting of an insulin peptide-MHC complex allows diabetogenic T cells to escape thymic deletion. J. Exp. Med. 2011, 208:2375-2383.
34. Sabatino J.J., et al. Manipulating antigenic ligand strength to selectively target myelin-reactive CD4+ T cells in EAE. J. Neuroimmune Pharmacol. 2010, 5:176-188.