Polymorphism at β85 and not β86 of HLA-DR1 is predominantly responsible for restricting the nature of the anchor side chain: Implication for concerted effects of class II MHC polymorphism

International Immunology

Volumn 9, Issue 10, 1997, Pages 1495-1502

  Wu, Shenhong ^a   Gorski, Jack ^b  

^a UNIVERSITY OF CHICAGO   (United States)

^b BLOOD RESEARCH INSTITUTE   (United States)

Author keywords

Insect cell; Peptide binding; Soluble HLA DR

Indexed keywords

ALANINE; HLA DR1 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; TRYPTOPHAN; TYROSINE;

AMINO ACID SUBSTITUTION; ANTIGEN BINDING; ARTICLE; CELL LINE; CONTROLLED STUDY; GENETIC POLYMORPHISM; HUMAN; INFLUENZA VIRUS; INSECT; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN POLYMORPHISM; PROTEIN STRUCTURE;

ALLELES; AMINO ACID SEQUENCE; ANIMALS; ANTIGENS; BINDING SITES; CELL LINE; GENES, MHC CLASS II; HLA-DR1 ANTIGEN; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POLYMORPHISM, GENETIC; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SOLUBILITY; SPODOPTERA;

EID: 0030822144     PISSN: 09538178     EISSN: None     Source Type: Journal    
DOI: 10.1093/intimm/9.10.1495     Document Type: Article

References (42)

1. Matzinger, P. 1993. Why positive selection? Immunol. Rev, 135:81.
2. Sherman, L. A. and Chattopadhyay, S. 1993. The molecular basis of allorecognition. Annu. Rev. Immunol. 11:385.
3. Winchester, R. and Dwyer, E. 1992. MHC and autoimmune diseases: susceptibility to rheumatoid arthritis associated with a hydrophobic strip of α-helix encoded by several MHC alleles. In Bona, C. and Kaushik, K., eds, Molecular Immunobiology of Self-reactivity, p. 203. Marcel Dekker, New York.
4. Nepom, G. T. 1991. MHC class II-molecules and autoimmunity. Annu. Rev. Immunol. 9:493.
5. Bjorkman, P. J., Saper, M. A., Smaraoui, B., Bennett, W. S., Strominger, J. L. and Wiley, D. C. 1987. Structure of the human class I histocompatibility antigen, HLA-A2. Nature 329:506.
6. Brown, J. H., Jardetzky, T. S., Gorga, J. C., Stern, L. J., Urban, R. G., Strominger, J. L. and Wiley, D. C. 1993. Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature 364:33.
7. Stern, L. J., Brown, J. H., Jardetzky, T. S., Gorga, J. C., Urban, R. G., Strominger, J. L. and Wiley, D. C. 1994. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 368:215.
8. Hammer J, Valsasnini, P., Tolba, K., Bolin, D., Higelin, J., Takacs, B. and Sinigaglia, F. 1993. Promiscuous and allele-specific anchors in HLA-DR-binding peptides. Cell 74:197.
9. Rotzschke, O. and Falk, K. 1994. Origin, structure and motifs of naturally processed MHC class II ligands. Curr. Opin. Immunol. 6:45.
10. Krieger, J. I., Karr, R. W., Grey, H. M., Yu, W., O'Sullivan, D., Batovsky, L., Zheng, Z., Colon, S. M., Gaeta, F. A., Sidney, J., Albertson, M., Guercio, M., Chestnut, R. W. and Sette, A. 1991. Single amino acid changes in DR and antigen define residues critical for peptide-MHC binding and T cell recognition. J. Immunol. 146:2331.
11. Racioppi, L., Ronchese, F., Schwartz, R. H. and Germain, R. N. 1991. The molecular basis of class II MHC allelic control of T cell responses. J. Immunol. 147:3718.
12. Garett, T. P. J., Saper, M. A., Bjorkman, P. J., Strominger, J. L. and Wiley, D. C. 1989. Specificity pockets for the side chains of peptide antigens in HLA-Aw68. Nature 342:692
13. Saper, M. A., Bjorkman, P. J. and Wiley, D. C. 1991. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J. Mol. Biol. 219:277.
14. Matsumura, M., Fremont, D. H., Peterson, P. A. and Wilson, I. A. 1992. Emerging principles for the recognition of peptide antigens by MHC class I molecules. Science 257:927.
15. Guo, H-C., Madden, D. R., Silver, M. L., Jardetzky, T. S., Gorga, J. C., Strominger, J. L. and Wiley, D. C. 1993. Comparison of the P2 specificity pocket in three human histocompatibility antigens, HLA-A*6801, HLA-A*0201, and HLA-B*2705. Proc. Natl Acad. Sci. USA 90:8053.
16. Young, A. C. M., Zhang, W., Sacchettini, J. C. and Nathenson, S, G. 1994. The three-dimensional structure of H-2Db at 2.4 Å resolution: implications for antigen-determinant selection. Cell 76:39.
17. Madden, D. R., Garboczi, D. N. and Wiley, D. C. 1993. The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75:693.
18. MHC class II database. histo.cryst.bbk.ac.uk/WWWFiles/sequences/sequence_map.html
19. Busch, R., Hill, C. M., Hayball, J. D., Lamb, J. R. and Rothbard, J. B. 1991. Effect of natural polymorphism at residue 86 of the HLA-DR β chain on peptide binding. J. Immunol. 147:1292.
20. Ong, B., Willcox, N., Wordsworth, P., Beeson, D., Vincent, A., Altman D., Lanchbury, H. S., Harcourt, G. C., Bell, J. I. and Newson-Davis, J. 1991. Critical role for the Val/Gly86 HLA-DRβ dimorphism in autoantigen presentation to human T cells. Proc. Natl Acad. Sci. USA 88:7343.
21. Demotz, S., Barbey, C., Corradin, G., Amoroso, A. and Lanzavecchia, A. 1993. The set of naturally processed peptides displayed by DR molecules is tuned by polymorphism of residue 86. Eur. J. Immunol. 23:425.
22. Zeliszewski, D., Golvano, J. J., Gaudebout, P., Dorval, I., Freidel, C., Gebuhrer, L., Betuel, H., Borras-Cuesta, F. and Sterkers, G. 1993. Implication of HLA-DR residues at positions 67, 71, and 86 in interaction between HLA-DR11 and peptide HA396-420. J. Immunol. 151:6237.
23. Geluk, A., Fu, X. T., Meijgaarden, K. E., Jansen, T. T. R., De Vries, R. R. P., Karr, R. W. and Ottenhoff, T. H. M. 1994. T cell receptor and peptide-contacting residues in the HLA-DR17 (3) β1 chain. Eur. J. Immunol. 24:324.
24. Fu XT., Bono, C. P., Woulfe, S. L., Swearingen, C., Summers, N. L., Sinigaglia, F., Sette, A., Schwartz, B. D. and Karr, R. W. 1995. Pocket 4 of the HLA-DR (alpha, beta 1*0401) molecule is a major determinant of T cells recognition of peptide. J. Exp. Med. 181:915.
25. Davernport, M. P., Quinn, C. L., Chicz, R. M., Green, B. N., Willis, A. C., Lane, W. S., Bell, J. I. and Hill, A. V. 1995. Naturally processed peptides from two disease-resistance-associated HLA-DR13 alleles show related sequence motifs and the effects of the dimorphism at position 86 of the HLA-DR beta chain. Proc. Natl Acad. Sci. USA 92:6567.
26. Posch P. E., Araujo, H. A., Creswell, K., Praud, C., Johnson, A. H. and Hurley, C. K. 1995. Microvariation creates significant functional differences in the DR3 molecules. Hum. Immunol. 42:61.
27. McKinney, J S., Fu, X. T., Swearingen, C., Klohe, E. and Karr, R. W. 1994. Individual effects of the DR11-variable β-chain residues 67, 71, and 86 upon DR (α,β1*1101)-restricted, peptide-specific T cell proliferation. J. Immunol. 153:5564.
28. Signorelli, K. L., Watts, L. M. and Lambert, L. E. 1995. The importance of DR4Dw4 beta chain residues 70, 71, and 86 in peptide binding and T cell recognition. Cell. Immunol. 162:217.
29. Newton-Nash, D. K. and Eckels, D. 1993. Differential effect of polymorphism at HLA-DR1 β-chain positions 85 and 86 on binding and recognition of DR1-restricted antigenic peptides. J. Immunol. 150:1813.
30. Wu, S., Gorski, J., Eckels, D. D. and Newton-Nash, D. K. 1996. T cell recognition of MHC class II-associated peptides is independent of peptide affinity for MHC and sodium dodecyl sulfate stability of the peptide/MHC complex. J. Immunol. 156:3815.
31. Stern, L. J. and Wiley, D. C. 1992. The human class II MHC protein HLA-DR1 assembles as empty αβ heterodimers in the absence of antigenic peptide. Cell 68:465.
32. Gorga, J. C., Horejsi, V., Johnson, D. R., Raghupathy, R. and Strominger, J. L. 1987. Purification and characterization of class II histocompatibility antigens from a homozygous human B cell line. J. Biol. Chem. 262:16087.
33. Jardetzky T. S., Gorga, J. C., Busch, R., Rothbard, J. B., Strominger, J. L. and Wiley, D. C. 1990. Peptide binding to HLA-DR1: a peptide with most residues substituted to alanine retains MHC binding. EMBO J. 9:1797.
34. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
35. Ghosh, P., Amaya, M., Mellins, E. and Wiley, D. C. 1995. The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature 378:457.
36. Panina-Bordignon, P., Tan, A., Termijtelen A., Demotz, S., Corradin, G. and Lanzavecchia, A. 1989. Universally immunogenic T cell epitopes: promiscuous binding to human MHC class II and promiscuous recognition by T cells. Eur. J. Immunol. 19:2237.
37. Geluk, A., van Meijgaarden, K. E., Southwood, S., Oseroff, C., Drijfhout, J. W., de Vries, R. R., Ottenhoff, T. H. and Sette, A. 1994. HLA-DR3 molecules can bind peptides carrying two alternative specific submotifs. J. Immunol 152:5742.
38. Sidney, J., Oseroff, C., Southwood, S., Wall, M., Ishioka, G., Koning, F. and Sette, A. 1992. DRB1*0301 molecules recognize a structural motif distinct from the one recognized by most DRβ1 alleles. J. Immunol. 149:2634.
39. Germain R. N. and Margulies, D. H., 1993. The biochemistry and cell biology of antigen processing and presentation. Annu. Rev. Immunol. 11:40.
40. Wu, S. and Gorski, J. 1996. The MHC class II associated invariant chain peptide CLIP binds to the peptide binding groove of class II molecules. Mol. Immunol. 33:371.
41. Verreck, F. A., Termijtelen, A. and Koning, F. 1993. HLA-DR beta chain residue 86 controls DR alpha beta dimer stability. Eur. J. Immunol. 23:1346.
42. Nagy, Z. A., Lehmann, P. V., Falcioni, F., Muller, S. and Adorini, L. 1989. Why peptides? Their possible role in the evolution of MHC-restricted T-cell recognition. Immunol. Today. 10:132.