The structure of cucumber mosaic virus: Cryoelectron microscopy, X-ray crystallography, and sequence analysis

Virology

Volumn 232, Issue 1, 1997, Pages 91-97

  Wikoff, William R ^a,b   Tsai, Chao Jo ^b   Wang, Guoji ^b   Baker, Timothy S ^b   Johnson, John E ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b PURDUE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CRYOELECTRON MICROSCOPY; CUCUMBER MOSAIC VIRUS; GENE SEQUENCE; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS; VIRUS GENE; VIRUS MORPHOLOGY; X RAY CRYSTALLOGRAPHY;

EID: 0342981744     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.8543     Document Type: Article

References (36)

1. Baker T. S., Newcomb W. W., Olson N. H., Corvsert L. M., Olson C., Brown J. C. Structures of bovine and human papillomaviruses. Biophys. J. 60:1991;1445-1456.
2. Bancroft J. B., Hills G. J., Markham R. A study of the self-assembly process in a small spherical virus: Formation of organized structures from protein subunitsin vitro. Virology. 31:1967;354-379.
3. Bancroft J. B. The self-assembly of spherical plant viruses. Adv. Virus Res. 16:1970;99-134.
4. Cheng R. H., Olson N. H., Baker T. S. Cauliflower mosaic virus: A 420 subunit (T. Virology. 186:1992;655-668.
5. Davies C., Symons R. H. Further implications for the evolutionary relationships between tripartite plant viruses based on cucumber mosaic virus RNA 3. Virology. 165:1988;216-224.
6. Francki R. I. B. Inactivation of cucumber mosaic virus (Q strain) nucleoprotein by pancreatic ribonuclease. Virology. 34:1968;694-700.
7. Genetics Computer Group, 1992, Program Manual for the GCG Package, Version 7.2.
8. Gorbalenya A. E., Koonin E. V. Comparative analysis of amino-acid sequences of key enzymes of replication and expression of positive-strand RNA viruses: Validity of approach and functional and evolutionary implications. Sov. Sci. Rev. D Physiochem. Biol. 11:1993;1-84.
9. Gorbalenya A. E., Blinov V. M., Donchenko A. P., Koonin E. V. An NTP-binding motif is the most conserved sequence in a highly diverged monophyletic group of proteins involved in positive strand RNA viral replication. J. Mol. Evol. 28:1989;256-268.
10. Harrison S. C. Virus structure: High-resolution perspectives. Adv. Virus Res. 28:1983;175-240.
11. Higgins D. G., Bleasby A. J., Fuchs R. CLUSTAL V: Improved software for multiple sequence alignment. Comput. Appl. Biosci. 8:1992;189-191.
12. Kabsch W. Automatic indexing of rotation diffraction patterns. J. Appl. Crystallogr. 21:1988a;67-71.
13. Kabsch W. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 21:1988b;916-924.
14. Lot H., Marrou J., Quiot J. B., Esvan C. Contribution à l'étude du virus de la mosaique du concombre. II. Methode de purification rapide du virus. Ann. Phytopathol. 4:1972;25-38.
15. Matthews B. W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
16. McPherson A. Preparation and Analysis of Protein Crystals. 1982;Wiley, New York.
17. F. A. Murphy, C. M. Faquet, D. H. L. Bishop, S. A. Ghabrial, A. W. Jarvis, G. P. Martelli, M. A. Mayo, M. D. Summers, 1995, Virus Taxonomy: Sixth Report of the International Committee on the Taxonomy of Viruses, Springer-Verlag, New York/Vienna.
18. O'Reilly D., Thomas C. J. R., Coutts R. H. A. Tomato aspermy virus has an evolutionary relationship with other tripartite RNA plant viruses. J. Gen. Virol. 72:1991;1-7.
19. Olson A. J., Bricogne G., Harrison S. C. Structure of tomato bushy stunt virus IV. The virus particle at 2.9 Å resolution. J. Mol. Biol. 171:1983;61-93.
20. Palukaitis P., Roossinck M. J., Shintaku M. H., Sleat D. E. Mapping functional domains in cucumber mosaic virus and its satellite RNAs. Can. J. Plant Pathol. 13:1991;155-162.
21. Perry K. L., Zhang L., Shintaku M. H., Palukatis P. Mapping determinants in cucumber mosaic virus for transmission byaphiz gossypil. Virology. 205:1994;591-595.
22. Rossmann M. G. The refinement of heavy-atom parameters in the presence of non-crystallographic symmetry. Acta Crystallogr. Sect. A. 32:1976;774-777.
23. Rossmann M. G. Processing oscillation diffraction data for very large unit cells with an automatic convolution technique and profile fitting. J. Appl. Crystallogr. 12:1979;225-235.
24. Rossmann M. G., Blow D. M. The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallogr. 15:1962;24.
25. Rossmann M. G., Leslie A. G. W., Abdel-Meguid S. S., Tsukihara T. Processing and post-refinement of oscillation camera data. J. Appl. Crystallogr. 12:1979;570-581.
26. Rost B., Sander C. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:1993;584-599.
27. Rost B., Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins. 19:1994;55-72.
28. Rost B., Sander C., Schneider R. PHD - An automatic mail server for protein secondary structure prediction. Comp. Appl. Biosci. 10:1994;53-60.
29. Sehnke P. C., Johnson J. E. Crystallization and preliminary X-ray characterization of tobacco streak virus and a proteolytically modified form of the capsid protein. Virology. 196:1993;328-331.
30. Speir J. A., Munshi S., Wang G., Baker T. S., Johnson J. E. Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo electron microscopy. Structure. 3:1995;63-78.
31. Speir J., Munshi S., Baker T. S., Johnson J. E. Preliminary X-ray data analysis of crystalline cowpea chlorotic mottle virus. Virology. 193:1993;234-241.
32. Shintaku M. Coat protein gene sequences of two cucumber mosaic virus strains reveal a single amino acid change correlating with chlorosis induction. J. Gen. Virol. 72:1991;2587-2589.
33. Smith T. J., Olson N. H., Cheng R. H., Chase E. S., Baker T. S. Structure of a human rhinovirus-bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility. Proc. Natl. Acad. Sci. USA. 90:1993;7015-7018.
34. van der Graaf M. Conformation and mobility of the RNA-binding N-terminal part of the intact coat protein of cowpea chlorotic mottle virus. A two-dimensional proton nuclear magnetic resonance study. J. Mol. Biol. 220:1991;701-709.
35. van der Graaf M., van Mierlo C. P. M., Hemminga M. A. Solution conformation of a peptide fragment representing a proposed RNA-binding site of a viral coat protein studied by two-dimensional NMR. Biochemistry. 30:1991;5722-5727.
36. Yusibov V., Kumar A., North A., Johnson J. E., Loesch-Fries L. S. Purification, characterization, virion assembly, and crystallization of alfalfa mosaic virus coat protein expressed inEscherichia coli. J. Gen. Virology. 77:1996;567-573.