Antagonist HIV-1 gag peptides induce structural changes in HLA B8

Journal of Experimental Medicine

Volumn 184, Issue 6, 1996, Pages 2279-2286

  Reid, Scott W ^a   McAdam, Steve ^b   Smith, Kathrine J ^b   Klenerman, Paul ^b   O'Callaghan, Chris A ^b   Harlos, Karl ^a,c   Jakobsen, Bent K ^b   McMichael, Andrew J ^b   Bell, John I ^b   Stuart, David I ^a,c   Jones, E Yvonne ^a,c  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b JOHN RADCLIFFE HOSPITAL   (United Kingdom)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; GAG PROTEIN; HLA B8 ANTIGEN; LIGAND; T LYMPHOCYTE RECEPTOR;

ANTIGEN PRESENTING CELL; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOTOXIC T LYMPHOCYTE; HUMAN; HUMAN CELL; MOLECULAR RECOGNITION; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; CELL LINE; CLONE CELLS; COMPUTER GRAPHICS; CRYSTALLOGRAPHY, X-RAY; GENE PRODUCTS, GAG; HIV-1; HLA-B8 ANTIGEN; HUMANS; IMMUNITY, CELLULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; T-LYMPHOCYTES, CYTOTOXIC; VARIATION (GENETICS);

EID: 12644251997     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.184.6.2279     Document Type: Article

References (36)

1. Bukrinsky, M.I., S. Haggerty, M.P. Dempsey, N. Sharova, A. Adzhubel, L. Spitz, P. Lewis, D. Goldfarb, M. Emerman, and M. Stevenson. 1993. A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cell. Nature (Lond.). 365:666-669.
2. Phillips, R.E., S. Rowland-Jones, D.F. Nixon, F.M. Gotch, J.P. Edwards, A.O. Ogunlesi, J.G. Elvin, J.A. Rothbard, C.R. Bangham, C.R. Rizza, et al. 1991. Human immunodeficiency virus genetic variation that can escape cytotoxic T cell recognition. Nature (Lond.). 354:453-459.
3. Nowak, M.A., R.M. May, R.E. Phillips, S. Rowland-Jones, D.G. Lalloo, S. McAdam, P. Klenerman, B. Koppe, K. Sigmund, C.R. Bangham, et al. 1995. Antigenic oscillations and shifting immunodominance in HIV-1 infections. Nature (Lond.). 375:606-611.
4. McAdam, S., P. Klenerman, L. Tussey, S. Rowland-Jones, D. Lalloo, R. Phillips, A. Edwards, P. Giangrande, A.L. Brown, F. Gotch, et al. 1995. Immunogenic HIV variant peptides that bind to HLA-B8 can fail to stimulate cytotoxic T lymphocyte responses. J. Immunol. 155:2729-2736.
5. Sutton, J., S. Rowland-Jones, W. Rosenberg, D. Nixon, F. Gotch, X.-M. Gao, N. Murray, A. Spoonas, P. Driscoll, M. Smith, A. Willis, and A. McMichael. 1993. A sequence pattern for peptides presented to cytotoxic T lymphocytes by HLA B8 Revealed by analysis of epitopes and eluted peptides. Eur. J. Immunol. 23:447-453.
6. Reid, S.W., K.J. Smith, B.K. Jakobsen, C.A. O'Callaghan, H. Reyburn, K. Harlos, D.I. Stuart, A. McMichael, J. Bell, and E.Y. Jones. 1996. Production and crystallization of MHC class I B allele single peptide complexes. FEBS Lett. 383: 119-123.
7. Moy, J.-P. 1994. A 200 mm input field, 5-80 keV detector based on and X-ray image intensifier and CCD camera. Nucl. Instr. Meth. A348:641-644.
8. Hammersley, A.P., S.O. Svensson, and A. Thompson. 1994. Calibration and correction of spatial distortions in 2D detector systems. Nucl. Instr. Meth. A346:312-321.
9. Otwinowski, Z. 1993. Oscillation data reduction program. In Data Collection and Processing. L. Sawyer, N. Isaacs, and S. Bailey, editors. Daresbury Laboratory, Warrington, UK. 55-62.
10. Brunger, A. 1992. A system for X-ray crystallography and NMR. In X-PLOR version 3.1. Yale University Press, New Haven, CT.
11. CCP4. 1994. The CCP4 Suite: programs for protein crystallography. Acta Crystallog. Sect. D Biol. Crystallog. 50:760-763.
12. Jones, A. 1985. Interactive computer graphics: FRODO. Methods Enzymol. 115:157-171.
13. Saper, M.A., P.J. Bjorkman, and D.C. Wiley. 1991. Refined structure of the human histocompatibility antigen HLA-2 at 2.6 A resolution. J. Mol. Biol. 219:277-319.
14. Madden, D.R., J.C. Gorga, J.L. Strominger, and D.C. Wiley. 1992. The three-dimensional structure of HLA-B27 at 2.1A resolution suggests a general mechanism for tight peptide binding to MHC. Cell. 70:1035-1048.
15. Silver, M.L., H.-C. Guo, J.L. Strominger, and D.C. Wiley. 1992. Atomic structure of a human MHC molecule presenting an influenza virus peptide. Nature (Lond.). 360:367-369.
16. Madden, D., D. Garboczi, and D. Wiley. 1993. The antigenic identity of peptide/MHC complexes: a comparison of the conformations of five peptides presented by HLA-2. Cell. 75:693.
17. Smith, K.J., S.W. Reid, K. Harlos, A. McMichael, D.I. Stuart, J. Bell, and E.Y. Jones. 1996. Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA B53. Immunity. 4: 215-228.
18. Smith, K.J., S.W. Reid, D.I. Stuart, A. McMichael, E.Y. Jones, and J. Bell. 1996. An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA B*3501. Immunity. 4:203-213.
19. Jameson, S.C., and M.J. Bevan. 1995. T cell receptor antagonists and partial agonists. Immunity. 2:1-11.
20. Lyons, D.S., S.A. Lieberman, J. Hampl, J.J. Boniface, Y.-H. Chien, L.J. Berg, and M.M. Davis. 1996. A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists. Immunity. 5:53-61.
21. McKeithan, T. 1995. Kinetic proofreading in T-cell receptor signal transduction. Proc. Natl. Acad. Sci. USA. 92:5042-5046.
22. Rabinowitz, J.D., C. Beeson, D.S. Lyons, M.M. Davis, and H.M. McConnell. 1996. Kinetic discrimination in T-cell activation. Proc. Natl. Acad. Sci. USA. 93:1401-1405.
23. Engh, R.A., and R. Huber. 1991. Accurate bond and angle parameters for X-ray protein-structure refinement. Acta. Crystallog. A47:392-400.
24. Bjorkman, P.L., 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 histocompatability antigens. Nature (Lond.). 329:512-518.
25. Bjorkman, P.J., M.A. Saper, B. Samraoui, W.S. Bennett, J.L. Strominger, and D.C. Wiley. 1987. Structure of the human class I histocompatability antigen, HLA-A2. Nature (Lond.). 329:506-512.
26. Garret, T.P.J., M.A. Saper, P.J. Bjorkman, J.L. Strominger, and D.C. Wiley. 1989. Specificity pockets for the side chains of peptide antigens in HLA-Aw68. Nature (Lond.). 342:692-696.
27. Madden, D.R., J.C. Gorga, J.L. Strominger, and D.C. Wiley. 1991. The structure of HLA-B27 reveals nonamer self-peptides bound in an extended confirmation. Nature (Lond.). 353:321-325.
28. Zhang, W., A.C. Young, M. Imarai, S.G. Nathenson, and J.C. Sacchettini. 1992. Crystal structure of the major histocompatibility complex class I H-2Kb molecule containing a single viral peptide: implications for peptide binding and T-cell receptor recognition. Proc. Natl. Acad. Sci. USA. 89:8403-8407.
29. Fremont, D.H., M. Matsumura, E.A. Stura, P.A. Peterson, and I.A. Wilson. 1992. Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb. Science (Wash. DC). 257:919-927.
30. 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: 927-934.
31. Guo, H.-C., T.S. Jardetzky, T.P.L. Garrett, W.S. Lane, J.L. Strominger, and D.C. Wiley. 1992. Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle. Nature (Lond.). 360:364-366.
32. Young, A.C.M., W. Zhang, J.C. Sacchettini, and S.G. Nathenson. 1994. The three-dimensional structure of H-2Db at 2.4A resolution: implications for antigen-determinant selection. Cell. 76:39-50.
33. Fremont, D., E. Stura, M. Matsumura, P. Peterson, and I. Wilson. 1995. Crystal structure of an H-2Kb-ovalbumin petide 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.
34. Kraulis, P.J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallography. 24:946-950.
35. Merritt, E.A., and M.E.P. Murphy. 1994. Raster 3D version 2.0. A program for photorealistic molecular graphics. Acta. Crystallog. Sec. D Biol. Crystallog. D50:869-873.
36. Stuart, D.I., M. Levine, M. Muirhead, and D. Stammers. 1979. The crystal structure of cat pyruvate kinase at a resolution of 2.6A. J. Mol. Biol. 134:109-142.