Crystal structure of the top domain of African horse sickness virus VP7: Comparisons with bluetongue virus VP7

Journal of Virology

Volumn 70, Issue 6, 1996, Pages 3797-3806

  Basak, Ajit K ^a,e   Gouet, Patrice ^a   Grimes, Jonathan ^a   Roy, Polly ^a,b,d   Stuart, David ^a,c  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b CENTRE FOR ECOLOGY AND HYDROLOGY   (United Kingdom)

^c UNIVERSITY OF OXFORD   (United Kingdom)

^d UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^e UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AFRICAN HORSE SICKNESS VIRUS; ARTICLE; BLUETONGUE ORBIVIRUS; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; VIRUS CELL INTERACTION; X RAY CRYSTALLOGRAPHY;

EID: 0029924725     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.6.3797-3806.1996     Document Type: Article

References (64)

1. Acharya, R., E. Fry, D. Stuart, C. Fox, D. Rowlands, and F. Brown. 1989. The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution. Nature (London) 337:709-716.
2. 1a.Artymiuk, P. Personal communication.
3. Bairoch, A. 1991. PROSITE: a dictionary of sites and patterns in protein. Nucleic Acids Res. 19:2241-2245.
4. Bairoch, A., and B. Boeckmann. 1990. The SWISSPROT protein sequence bank. Nucleic Acids Res. 19:2247-2248.
5. 3a.Basok, A. K., et al. Unpublished results.
6. Brünger, A. T., J. Kuriyan, and M. Karplus. 1987. Crystallographic Rfactor refinement by molecular dynamic. Science 235:23-28.
7. Burroughs, J. N., R. S. O'Hara, C. J. Smale, C. Hamblin, A. Walton, R. Armstrong, and P. P. C. Mertens. 1994. Purification and properties of virus particles, infectious subviral particles cores and VP7 crystals of African horsesickness virus serotype 9. J. Gen. Virol. 78:1849-1857.
8. 5a CCP4. 1979. The SERC (UK) collaborative computing project no. 4, a suite of programs for protein crystallography. Daresbury Laboratory, Warrington, United Kingdom.
9. Chotia, C., and A. M. Lesk. 1986. The relation between the divergence of sequence and structure in proteins. EMBO J. 5:823-826.
10. Chuma, T., H. Le Blois, J. M. Sanchez Vizcaino, M. Diaz Laviada, and P. Roy. 1992. Expression of the major core antigen VP7 of African horsesickness virus by a recombinant baculovirus and its use as a group-specific diagnostic reagent. J. Gen. Virol. 73:925-931.
11. 7a.Collaboralive Computational Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. A 47:110-119.
12. Connolly, M. L. 1983. Solvent-accessible surfaces of proteins and nucleic acids. Science 221:709-713.
13. Dyda, F., A. B. Hickman, T. M. Jenkins, A. Engelman, R. Craigie, and D. R. Davies. 1994. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science 256:1946.
14. Eaton, B. T., A. R. Gould, A. D. Hyatt, B. E. H. Coupar, J. C. Martyn, and J. R. White. 1991. A bluetongue serogroup-reactive epitope in the amino terminal half of the major protein VP7 is accessible on the surface of bluetongue virus particles. Virology 180:687-696.
15. Fox, G., N. R. Parry, P. V. Barnett, B. McGinn, D. J. Rowlands, and F. Brown. 1989. The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (arginine-glycine-aspartic acid). J. Gen. Virol. 70:625-637.
16. French, T. J., J. J. A. Marshall, and P. Roy. 1990. Assembly of double-shelled, viruslike particles of bluetongue virus by the simultaneous expression of four structural proteins. J. Virol. 64:5695-5700.
17. French, T. J., and P. Roy. 1990. Synthesis of bluetongue virus (BTV) corelike particles by a recombinant baculovirus expressing the two major structural core proteins of BTV. J. Virol. 64:1530-1536.
18. Grimes, J. 1995. Structural studies on bluetongue virus. Ph.D. thesis. Oxford University.
19. Grimes, J., A. K. Basak, P. Roy, and D. Stuart. 1995. The crystal structure of bluetongue virus VP7. Nature (London) 373:167-170.
20. 15a.Grimes, J., and D. Stuart. Unpublished program.
21. Howell, P. G. 1962. The isolation and identification of further antigenic types of African horsesickness virus. Onderstepoort. J. Vet. Res. 29:139-149.
22. Hutchinson, E. G., and J. M. Thornton. 1990. HERA - a program to draw schematic diagrams of protein secondary structures. Proteins Struct. Fund. Genet. 8:203-212.
23. Iwata, H., T. Chuma, and P. Roy. 1992. Characterization of genes encoding two of the major capsid proteins of epizootic haemorrhagic disease virus indicates a close genetic relationship to bluetongue virus. J. Gen. Virol. 73:915-925.
24. Jancarik, J., and S. H. Kim. 1991. Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24:409-411.
25. Jones, E. Y., K. Harlos, M. J. Bottomley, R. C. Robinson, P. C. Driscoll, R. M. Edwards, J. M. Clements, T. J. Dudgeon, and D. I. Stuart. 1995. Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 Å resolution. Nature (London) 373:539-544.
26. Jones, E. Y., and D. I. Stuart. 1991. Locating heavy atom sites by automatic Patterson search - GROPAT, p. 39-47. In W. Wolf, P. R. Evans, and A. G. W. Leslie (ed.), Isomorphous replacement and anomalous scattering. Science and Engineering Research Council, Warrington, United Kingdom.
27. Kabsch, W. 1988. Automatic indexing of rotation diffraction patterns. J. Appl. Crystallogr. 21:67-71.
28. Kabsch, W. 1988. Evaluation of single crystal X-ray diffraction data from a position sensitive detector. J. Appl. Crystallogr. 21:916-924.
29. Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
30. Kleywegt, G., and T. A. Jones. 1994. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr. Sect. D 50:178-185.
31. Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24:946-950.
32. Kyte, J., and R. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
33. Laviada, M. D., P. Roy, and J. M. Sanchez-Vizcaino. 1992. Adaptation and evaluation of an indirect ELISA and immunoblotting test for African horsesickness antibody detection, p. 646-650. In T. E. Walton and B. I. Osburn (ed.), Bluetongue African horsesickness and related orbiviruses. CRC Press, Boca Raton, Fla.
34. Le Blois, H., and P. Roy. 1993. A single point mutation in the VP7 major core protein of bluetongue virus prevents the formation of core-like particles. J. Virol. 67:353-359.
35. Lee, J., P. Rieu, M. A. Arnaout, and R. Liddington. 1995. Crystal structure of the A domain from the a subunit of integrin CR3 (GD11b/CD18). Cell 80:631-638.
36. Leslie, A. G. W. 1987. Profile fitting, p. 39-50. In J. H. Helliwell, P. A. Machin, and M. Z. Papiz (ed.), Computational aspect of protein crystal data analysis. SERC, Daresbury Laboratory, Warrington, United Kingdom.
37. Logan, D., R. Abu-Ghazaleh, W. Blakemore, S. Curry, T. Jackson, A. King, S. Lea, R. Lewis, J. Newman, N. Parry, D. Rowlands, D. Stuart, and E. Fry. 1993. Structure of a major immunogenic site on foot-and-mouth disease virus. Nature (London) 362:566-568.
38. Lubroth, J. 1988. African horsesickness and the epizootic in Spain 1987. Equine Pract. 10:26-33.
39. Luzatti, V. 1952. Traitement statistique des erreurs dans la détermination des structures cristallines. Acta Crystallogr. 5:802-810.
40. Mason, P. W., E. Rieder, and B. Baxt. 1994. ROD sequence of foot-and-mouth disease virus is essential for infecting cells via the natural receptor but can be bypassed by an antibody-dependent enhancement pathway. Proc. Natl. Acad. Sci. USA 91:1932-1936.
41. Matthews, B. W. 1985. Determination of protein molecular weight, hydration, and packing from crystal density. Methods Enzymol. 114:176-187.
42. McIntosh, B. M. 1958. Immunological types of horsesickness virus and their significance in immunization. Onderstepoort J. Vet. Res. 27:465-538.
43. McPherson, A. J. 1982. Preparation and analysis of protein crystals, p. 82-160. John Wiley and Sons, New York.
44. Mellor, P. 1993. African horsesickness transmission and epidemiology. Vet. Res. 24:199-212.
45. Merrit, E. A., and M. E. P. Murphy. 1994. Raster3D version 2.0. A program for photo-realistic molecular graphics. Acta Crystallogr. Sect. D 50:869-873.
46. 40a.Mertens, P. P. C. Personal communication.
47. Mertens, P. P. C., J. N. Burroughs, H. Fu, M. P. Wellby, D. M. Jennings, R. S. O'Hara, A. Walton, and P. S. Mellor. Enhanced infectivity of modified bluetongue virus particles for Culicoides vectors and to infect cell lines. Virology, in press.
48. Murphy, F. A., E. C. Borden, R. E. Shope, and A. Harrison. 1971. Physicochemical and morphological relationships of some arthropod-borne viruses to bluetongue virus - a new taxonomic group. Electron microscopic studies. J. Gen. Virol. 13:273-288.
49. Navaza, J. 1992. AMoRe: a new package for molecular replacement, p. 87-90. In E. J. Dodson, S. Gover, and W. Wolf (ed.), Molecular replacement. SERC, Daresbury Laboratory, Warrington, United Kingdom.
50. Otwinowski, Z. 1991. Maximum likelihood refinement of heavy atom parameters, p. 80-85. In W. Wolf, P. R. Evans, and A. G. W. Leslie (ed.), Isomorphous replacement and anomalous scattering. SERC. Daresbury Laboratory, Warrington, United Kingdom.
51. Otwinowski, Z. 1993. Oscillation data reduction program, p. 56-62. In L. Sawyer, N. Isaac, and S. Bailey (ed.), Data collection and processing. SERC, Daresbury Laboratory, Warrington, United Kingdom.
52. Pierschbacher, M. D., and E. Ruoslahti. 1984. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature (London) 309:30-33.
53. Prasad, B. V. V., S. Yamaguchi, and P. Roy. 1992. Three-dimensional structure of single-shelled bluetongue virus. J. Virol. 66:2135-2142.
54. Robinson, I. K., and S. C. Harrison. 1982. Structure of the expanded state of tomato bushy stunt virus. Nature (London) 297:563-568.
55. Rossmann, M. G., et al. 1985. Structure of a human common cold virus and functional relationship to other picornaviruses. Nature (London) 317:145-153.
56. Roussel, A., and C. Cambillau. 1989. TURBO-FRODO, p. 77-78. In Silicon Graphics (ed.), Silicon graphics geometry partner directory. Silicon Graphics, Mountain View, Calif.
57. Roy, P. 1992. Bluetongue virus proteins. J. Gen. Virol. 73:3051-3064.
58. Roy, P. Orbiviruses and their replication. In B. N. Fields (ed.), Virology, in press. Raven Press, New York.
59. Roy, P., T. Hirasawa, M. Fernandez, V. M. Blinov, and J. M. Sanchez-Vixcaino Rodrique. 1991. The complete sequence of the group-specific antigen, VP7, of African horsesickness disease virus serotype 4 reveals a close relationship to bluetongue virus. J. Gen. Virol. 72:1237-1241.
60. Roy, P., J. J. Marshall, and T. J. French. 1990. Structure of the bluetongue virus genome and its encoded proteins. Curr. Top. Microbiol. Immunol. 162: 43-87.
61. Ruoslahti, E. 1988. Fibronectin and its receptors. Annu. Rev. Biochem. 57: 375-413.
62. Sakabe, N. 1991. X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instr. Methods Phys. Res. 303:448-463.
63. Stuart, D. I., and E. Y. Jones. 1993. Weissenberg data collection for macro-molecular crystallography. Curr. Opin. Struct. Biol. 3:737-740.
64. Zlotnick, A., V. S. Reddy, R. Dasgupta, A. Schneemann, W. J. Ray, Jr., R. R. Rueckert, and J. E. Johnson. 1994. Capsid assembly in a family of animal viruses primes an autoproteolytic maturation that depends on a single aspartic acid residue. J. Biol. Chem. 269:13680-13684.