T cell receptor (TCR) recognition of MHC class I variants: Intermolecular second-site reversion provides evidence for peptide/MHC conformational variation

Journal of Experimental Medicine

Volumn 184, Issue 1, 1996, Pages 253-258

  Dyall, Ruben ^a,b   Fremont, Daved H ^c,d   Jameson, Stephen C ^e   Nikolić Žugić, Janko ^a,b  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^b Weill Cornell Graduate School of Biomedical Sciences   (United States)

^c Och Spine at New York Presbyterian Hospitals   (United States)

^d NATIONAL JEWISH MEDICAL AND RESEARCH CENTER   (United States)

^e UNIVERSITY OF MINNESOTA MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN; T LYMPHOCYTE RECEPTOR;

ANIMAL CELL; ANTIGEN PRESENTATION; ANTIGEN RECOGNITION; ARTICLE; CONFORMATIONAL TRANSITION; HYDROGEN BOND; MAJOR HISTOCOMPATIBILITY COMPLEX; MOLECULAR MODEL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; T LYMPHOCYTE RECEPTOR GENE;

AMINO ACID SEQUENCE; ANIMALS; ANTIGEN-PRESENTING CELLS; ANTIGENS, VIRAL; BINDING SITES; H-2 ANTIGENS; MICE; MICE, INBRED C57BL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OVALBUMIN; PEPTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; RECEPTORS, ANTIGEN, T-CELL; SIMPLEXVIRUS; STRUCTURE-ACTIVITY RELATIONSHIP; T-LYMPHOCYTES, CYTOTOXIC;

EID: 0030018187     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.184.1.253     Document Type: Article

References (30)

1. Lawlor, D.A., J. Zemmour, P.D. Ennis, and P. Parham. 1990. Evolution of class I-MHC genes and proteins. Annu. Rev. Immunol. 8:23-63.
2. Ajitkumar, P., S.S. Geier, K.V. Kesari, F. Borriello, M. Nakagawa, J.A. Bluestone, M.A. Saper, D.C. Wiley, and S.G. Natheson. 1988. Evidence that multiple residues on both the α-helices of the Class I MHC molecule are simultaneously recognized by the T cell receptor. Cell. 54:47-56.
3. Grandea, A.G., III, and M.J. Bevan. 1992. Single-residue changes in class I major histocompatibility complex molecules stimulate responses to self-peptides. Proc. Natl. Acad. Sci. USA. 89:2794-2798.
4. Rammensee, H.-G., T. Friede, and S. Stevanović. 1995. MHC ligands and peptide motifs: first listing, Immunogenetics. 41:178-228.
5. Nikolić-Žugić, J., and F.R. Carbone. 1991. Peptide presentation by class-I major histocompatibility complex molecules. Immunol. Res. 10:54-65.
6. Chattopadhyay, S., T. Matthias, J. Biggs, and L.A. Sherman. 1994. Conformational differences in major histocompatibility complex-peptide complexes can result in alloreactivity. J. Exp. Med. 179:213-219.
7. Dyall, R., L.V. Vasovic, A. Molano, and J. Nikolić-Žugić. 1995. CD4-independent in vivo priming of murine CTLs by optimal MHC class I-restricted peptides derived from HIV and other pathogens. Int. Immunol. 7:1205-1212.
8. b restricted ovalbumin peptide and an assessment of the predictive power of MHC binding motifs. Eur. J. Immunol. 22:2663-2669.
9. Carson, M. 1987. Ribbon models of macromolecules. J. Mol. Graphics. 5:103-106.
10. Jones, T.A. 1978. A graphics model building and refinement system for macromolecules. J. Appl. Cryst. 11:268-272.
11. b-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove. Proc. Natl. Acad. Sci. USA. 92: 2479-2483.
12. b. Science (Wash. DC). 257:919-926.
13. Saito, Y., P.A. Peterson, and M. Matsumura. 1993. Quantitation of peptide anchor residue contributions to class I major histocompatibility complex molecule binding. J. Biol. Chem. 268:21309-21317.
14. Chen, W., J. McCluskey, S. Rodda, and F.R. Carbone. 1993. Changes at peptide residues buried in the major histocompatibility complex (MHC) class I binding cleft influence T cell recognition: a possible role for indirect conformational alterations in the MHC class I or bound peptide in determining T cell recognition. J. Exp. Med. 177:869-873.
15. b. Int. Immunol. 6:1037-1047.
16. Nikoli-Žugić, J., and M.J. Bevan. 1990. Role of self-peptides in positively selecting the T-cell repertoire. Nature (Lond.). 344:65-67.
17. Nikolić-Žugić, J., and R. Dyall. 1993. Positive selection of the T-cell repertoire is affected by mutations in the peptide-binding site of MHC class I molecules. Ann. NY Acad. Sci. 681:16-24.
18. Nathenson, S.G., J. Geliebter, G.M. Pfaffenbach, and R.A. Zeff. 1986. Murine major histocompatibility complex class I mutants. Annu. Rev. Immunol. 4:471-502.
19. Bjorkman, P.J., M.A. Saper, B. Samraoui, W.S. Bennett, J.L. Strominger, and D.C. Wiley. 1987. The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens. Nature (Lond.). 329:512-518.
20. b molecule containing a single viral peptide: implications for peptide binding and T-cell receptor recognition. Proc. Natl. Acad. Sci. USA. 89: 8403-8407.
21. b antigen recognition site. J. Immunol. 146:2145-2151.
22. Rohren, E.M., L.R. Pease, H.L. Ploegh, and T.N.M. Schumacher. 1993. Polymorphisms in pockets of major histocompatibility complex class I molecules influence peptide preference. J. Exp. Med. 177:1713-1721.
23. Poteete, A.R., D.P. Sun, H. Nicholson, and B.W. Matthews. 1991. Second-site revertants of an inactive T4 lysozyme mutant restore activity by restructuring the active site cleft. Biochemistry. 30:1425-1432.
24. Nelson, E.R., and M.G. Douglas. 1993. Function-based mapping of the yeast mitochondrial ADP/ATP translocator by selection for second site revertants. J. Mol. Biol. 230:1171-1182.
25. Matsumura, M., D.H. Fremont, P.A. Peterson, and I.A. Wilson. 1992. Emerging principles for the recognition of peptide antigens by MHC class-I molecules. Science (Wash. DC). 257: 927-932.
26. Guo, H-C., D.R. Madden, M.L. Silver, T.S. Jardetzky, J.C. Gorga, J.L. Strominger, and D.C. Wiley. 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. 90:8053-8057.
27. Madden, D.R., D.N. Garboczi, and D.C. Wiley. 1993. The antigenic identify of peptide-MHC complexes: a comparison of conformations of five viral peptides presented by HLA-A2. Cell. 75:693-708.
28. Ćatipović, B., J. Dal Porto, M. Mage, T.E. Johansen, and J.P. Schneck. 1992. Major histocompatibility complex conformational epitopes are peptide specific. J. Exp. Med. 176: 1611-1618.
29. Bluestone, J.A., S. Jameson, S. Miller, and R.I. Dick. 1992. Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition. J. Exp. Med. 176:1611-1618.
30. Hogquist, K.A., A.G. Grandea, III, and M.J. Bevan. 1993. Peptide variants reveal how antibodies recognize major histocompatibility complex class I. Eur. J. Immunol. 23:3028-3036.