Structures of T = 1 and T = 3 Particles of Cucumber Necrosis Virus: Evidence of Internal Scaffolding

Journal of Molecular Biology

Volumn 365, Issue 2, 2007, Pages 502-512

  Katpally, Umesh ^a   Kakani, Kishore ^b   Reade, Ron ^b   Dryden, Kelly ^c   Rochon, D'Ann ^b   Smith, Thomas J ^a  

^a DONALD DANFORTH PLANT SCIENCE CENTER   (United States)

^b AGRICULTURE AND AGRI FOOD CANADA   (Canada)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

cryo TEM; cucumber necrosis virus; scaffold; structure; virus

Indexed keywords

CAPSID PROTEIN; PROTEIN SUBUNIT; VIRUS PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CUCUMBER NECROSIS VIRUS; MUTAGENESIS; NEUTRON SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TOMBUSVIRUS; VIRUS CAPSID; VIRUS MORPHOLOGY; VIRUS PARTICLE;

CUCUMBER NECROSIS VIRUS; MIRIDAE; TOMATO BUSHY STUNT VIRUS; TOMBUSVIRUS;

EID: 33751538861     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.09.060     Document Type: Article

References (39)

1. Rochon D.M., and Tremaine J.H. Complete nucleotide sequence of the cucumber necrosis virus genome. Virology 71 (1989) 251-259
2. Rochon D., Kakani K., Robbins M., and Reade R. Molecular aspects of plant virus transmission by Olpidium and Plasmodiophorid vectors. Annu. Rev. Phytopathol. 42 (2004) 211-241
3. Harrison S.C., Olson A.J., Schutt C.E., Winkler F.K., and Bricogne G. Tomato bushy stunt virus at 2.9 Å resolution. Nature 276 (1978) 368-373
4. Xiang Y., Kakani K., Hui E., and Rochon D. A 38 amino acid sequence encompassing the arm domain of the cucumber necrosis virus coat protein functions as a chloroplast transit peptide in infected plants. J. Virol. 80 (2006) 7952-7964
5. Campbell R.N. Fungal transmission of plant viruses. Annu. Rev. Phytopath. 34 (1996) 87-108
6. Dias H.F. The relationship between cucumber necrosis virus by Olpidium cucurbitacaerum. Virology 40 (1970) 828-839
7. Chauvin C., Witz J., and Jacrot B. Structure of the tomato bushy stunt virus: a model for protein-RNA interactions. J. Mol. Biol. 124 (1978) 641-651
8. Timmins P.A., Wild D., and Witz J. The three-dimensional distribution of RNA and protein in the interior of tomato bushy stunt virus: a neutron low-resolution single-crystal diffraction study. Structure 2 (1994) 1191-1201
9. Hui E., and Rochon D. Evaluation of specific regions of the cucumber necrosis virus coat protein arm on particle accumulation and fungus transmission. J. Virol. 80 (2006) 5968-5975
10. Hsu C., Singh P., Ochoa W., Manayani D.J., Manchester M., Schneeman A., and Reddy V.S. Characterization of polymorphism displayed by the coat protein of mutants of tomato bushy stunt virus. Virology 349 (2006) 222-229
11. Larson S.B., Lucas R.W., and McPherson A. Crystallographic structure of the T = 1 particle of brome mosaic virus. J. Mol. Biol. 346 (2005) 815-831
12. Sangita V., Lokesh G.L., Satheshkumar P.S., Vijay C.S., Saravanan V., Savithri H.S., and Murthy M.R.N. T = 1 capsid structures of sesbania mosaic virus coat protein mutants: determinants of T = 3 and T = 1 capsid assembly. J. Mol. Biol. 342 (2004) 987-999
13. Kakani K., Reade R., and Rochon D. Evidence that vector transmission of a plant virus requires conformational change in virus particles. J. Mol. Biol. 338 (2004) 507-517
14. Lewis J.K., Bothner B., Smith T.J., and Siuzdak G. Antiviral agent blocks breathing of the common cold virus. Proc. Natl Acad. Sci. USA 95 (1998) 6774-6778
15. Reisdorph N., Thomas J., Katpally U., Chase E., Harris K., Siuzdak G., and Smith T.J. Human rhinovirus capsid dynamics is controlled by canyon flexibility. Virology 314 (2003) 34-44
16. Harrison S.C., and Jack A. Structure of tomato bushy stunt virus. III. Three dimensional X-ray diffraction analysis at 16 Å resolution. J. Mol. Biol. 97 (1975) 173-191
17. Chen Z., Stauffacher C., Li Y., Schmidt T., Bomu W., Kamer G., et al. Protein-RNA interactions in an icosahedral virus at 3.0 Å resolution. Science 245 (1989) 154-159
18. Tihova M., Dryden K.A., Le T.L., Harvey S.C., Johnson J.E., Yeager M., and Schneemann A. Nodavirus coat protein imposes dodecahedral RNA structure independent of nucleotide sequence and length. J. Virol. 78 (2004) 2897-2905
19. Tang L., Johnson K.N., Ball L.A., Lin T., Yeager M., and Johnson J.E. The structure of Pariacoto virus reveals a dodecahedral cage of duplex RNA. Nature Struct. Biol. 8 (2001) 77-83
20. Bergdoll M., Remy M.-H., Cagnon C., Masson J.-M., and Dumas P. Proline dependent oligomerization with arm exchange. Structure 5 (1997) 391-401
21. Robbins M.A., Reade R.D., and Rochon D.M. A cuccumber necrosis virus variant deficient in fungal transmissibility contains an altered coat protein shell domain. Virology 234 (1997) 138-146
22. Kakani K., Sgro J.-Y., and Rochon D. Identification of specific cumber necrosis virus coat protein amino acids affecting fungus transmission and zoospore attachment. J. Virol. 75 (2001) 5576-5583
23. Kakani K., Robbins M., and Rochon D. Evidence that binding of cucumber necrosis virus to vector zoospores involves recognition of oligosaccharides. J. Virol. 77 (2003) 3922-3928
24. Smith T.J. MolViewX: a molecular visualization program for the Macintosh OS X system. J. Appl. Crystallog. 37 (2004) 654-657
25. Pettersen E.F., Goddard T.D., Huang C.C., Couch G.S., Greenblatt D.M., Meng E.C., and Ferrin T.E. UCSF chimera - a visualization system for exploratory research and analysis. J. Comput. Chem. 25 (2004) 1605-1612
26. Baker T.S., Olson N.H., and Fuller S.D. Adding the third dimension to virus life cycles: Three-Dimensional reconstruction of icosahedral viruses from cryo-electron micrographs. Microbiol. Mol. Biol. Rev 63 (1999) 862-922
27. Suloway C., Pulokas J., Fellmann D., Cheng A., Guerra F., Quispe J., et al. Automated molecular microscopy: the new Leginon system. J. Struc. Biol. 151 (2005) 41-60
28. Conway J.F., Duda R.L., Cheng N., Hendrix R.W., and Steven A.C. Proteolytic and conformational control of virus capsid maturation: the bacteriophage HK97 system. J. Mol. Biol. 253 (1995) 86-99
29. Conway J.F., and Steven J.M. Methods for reconstructing density maps of "single" particles from cryoelectron micrographs to subnanometer resolution. J. Struct. Biol. 128 (1999) 106-118
30. Conway J.F., Trus B.L., Booy F.P., Newcomb W.W., Brown J.C., and Steven A.C. The effects of radiation damage on the structure of frozen hydrated HSV1 capsids. J. Struct. Biol. 111 (1993) 222-233
31. Heymann J.B. Bsoft: image and molecular processing in electron microscopy. J. Struct. Biol. 133 (2001) 156-169
32. Baker T.S., and Cheng R.H. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116 (1996) 120-130
33. Bubeck D., Filman D.J., Cheng N., Steven A.C., Hogle J.M., and Belnap D.M. The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. J. Virol. 79 (2005) 7745-7755
34. Crowther R.A., Amos L.A., Finch J.T., De Rosier D.J., and Klug A. Three dimensional reconstructions of spherical viruses by fourier synthesis from electron micrographs. Nature 226 (1970) 421-425
35. Brunger A.T., Adams P.D., Clore G.M., Gros P., Grosse-Kunstleve R.W., Jiang J.-S., et al. Crystallography & NMR system (CNS): a new software system for macromolecular structure determination. Acta Crystallog sect. D 54 (1998) 905-921
36. Winkler F.K., Schutt C.E., and Harrison S.C. Tomato bushy stunt virus at 5.5-Å resolution. Nature 265 (1977) 509-513
37. Jones T.A., Zou J.-Y., and Cowan S.W. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog sect. A 47 (1991) 110-119
38. Che Z., Olson N.H., Leippe D., Lee W.-M., Mosser A., Rueckert R.R., et al. Antibody-mediated neutralization of human rhinovirus 14 explored by means of cryo-electron microscopy and X-ray crystallography of virus-Fab complexes. J. Virol. 72 (1998) 4610-4622
39. Collaborative computational project, n. The CCP4 suite: Programs for protein crystallography. Acta Crystallog sect. D 50 (1994) 760-763