This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lu, G.
Right arrow Articles by Chiu, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lu, G.
Right arrow Articles by Chiu, W.

 Previous Article  |  Next Article 

Journal of Virology, November 1998, p. 8541-8549, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Structure of Double-Shelled Rice Dwarf Virus

Guangying Lu,1 Z. Hong Zhou,2 Matthew L. Baker,3 Joanita Jakana,4 Deyou Cai,1 Xincheng Wei,1 Shengxiang Chen,5 Xiaocheng Gu,1 and Wah Chiu3,4,*

National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871,1 and Zhejiang Academy of Agricultural Sciences, Hangzhou 310021,5 China, and Department of Pathology and Laboratory Medicine, University of Texas--- Houston Medical School,2 and Program in Structural and Computational Biology and Molecular Biophysics3 and Verna and Marrs McLean Department of Biochemistry,4 Baylor College of Medicine, Houston, Texas 77030

Received 10 February 1998/Accepted 14 July 1998

Rice dwarf virus (RDV), a member of the Reoviridae family, is a double-stranded RNA virus. Infection of rice plants with RDV reduces crop production significantly and can pose a major economic threat to Southeast Asia. A 25-Å three-dimensional structure of the 700-Å-diameter RDV capsid has been determined by 400-kV electron cryomicroscopy and computer reconstruction. The structure revealed two distinctive icosahedral shells: a T=13l outer icosahedral shell composed of 260 trimeric clusters of P8 (46 kDa) and an inner T=1 icosahedral shell of 60 dimers of P3 (114 kDa). Sequence and structural comparisons were made between the RDV outer shell trimer and the two crystal conformations (REF and HEX) of the VP7 trimer of bluetongue virus, an animal analog of RDV. The low-resolution structural match of the RDV outer shell trimer to the HEX conformation of VP7 trimer has led to the proposal that P8 consists of an upper domain of beta -sandwich motif and a lower domain of alpha  helices. The less well fit REF conformation of VP7 to the RDV trimer may be due to the differences between VP7 and P8 in the sequence of the hinge region that connects the two domains. The additional mass density and the absence of a known signaling peptide on the surface of the RDV outer shell trimer may be responsible for the different interactions between plants and animal reoviruses.

* Corresponding author. Mailing address: Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030. Phone: (713) 798-6985. Fax: (713) 796-9438. E-mail: wah{at}bcm.tmc.edu.

Journal of Virology, November 1998, p. 8541-8549, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Chen, T., Zhang, Z., Glotzer, S. C. (2007). A precise packing sequence for self-assembled convex structures. Proc. Natl. Acad. Sci. USA 104: 717-722 [Abstract] [Full Text]  
  • Li, Y., Tan, L., Li, Y., Chen, W., Zhang, J., Hu, Y. (2006). Identification and genome characterization of Heliothis armigera cypovirus types 5 and 14 and Heliothis assulta cypovirus type 14. J. Gen. Virol. 87: 387-394 [Abstract] [Full Text]  
  • Adamson, W. E., McNab, D., Preston, V. G., Rixon, F. J. (2006). Mutational Analysis of the Herpes Simplex Virus Triplex Protein VP19C. J. Virol. 80: 1537-1548 [Abstract] [Full Text]  
  • Pous, J., Chevalier, C., Ouldali, M., Navaza, J., Delmas, B., Lepault, J. (2005). Structure of birnavirus-like particles determined by combined electron cryomicroscopy and X-ray crystallography. J. Gen. Virol. 86: 2339-2346 [Abstract] [Full Text]  
  • Limn, C.-K., Roy, P. (2003). Intermolecular Interactions in a Two-Layered Viral Capsid That Requires a Complex Symmetry Mismatch. J. Virol. 77: 11114-11124 [Abstract] [Full Text]  
  • Caston, J. R., Martinez-Torrecuadrada, J. L., Maraver, A., Lombardo, E., Rodriguez, J. F., Casal, J. I., Carrascosa, J. L. (2001). C Terminus of Infectious Bursal Disease Virus Major Capsid Protein VP2 Is Involved in Definition of the T Number for Capsid Assembly. J. Virol. 75: 10815-10828 [Abstract] [Full Text]  
  • Zheng, H., Yu, L., Wei, C., Hu, D., Shen, Y., Chen, Z., Li, Y. (2000). Assembly of Double-Shelled, Virus-Like Particles in Transgenic Rice Plants Expressing Two Major Structural Proteins of Rice Dwarf Virus. J. Virol. 74: 9808-9810 [Abstract] [Full Text]  
  • Nason, E. L., Samal, S. K., Venkataram Prasad, B. V. (2000). Trypsin-Induced Structural Transformation in Aquareovirus. J. Virol. 74: 6546-6555 [Abstract] [Full Text]  
  • Baker, T. S., Olson, N. H., Fuller, S. D. (1999). Adding the Third Dimension to Virus Life Cycles: Three-Dimensional Reconstruction of Icosahedral Viruses from Cryo-Electron Micrographs. Microbiol. Mol. Biol. Rev. 63: 862-922 [Abstract] [Full Text]  
  • Zhang, H., Zhang, J., Yu, X., Lu, X., Zhang, Q., Jakana, J., Chen, D. H., Zhang, X., Zhou, Z. H. (1999). Visualization of Protein-RNA Interactions in Cytoplasmic Polyhedrosis Virus. J. Virol. 73: 1624-1629 [Abstract] [Full Text]  
  • Zhou, Z. H., Liao, W., Cheng, R. H., Lawson, J. E., McCarthy, D. B., Reed, L. J., Stoops, J. K. (2001). Direct Evidence for the Size and Conformational Variability of the Pyruvate Dehydrogenase Complex Revealed by Three-dimensional Electron Microscopy. THE "BREATHING" CORE AND ITS FUNCTIONAL RELATIONSHIP TO PROTEIN DYNAMICS. J. Biol. Chem. 276: 21704-21713 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»