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 Neuman, B. W.
Right arrow Articles by Buchmeier, M. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Neuman, B. W.
Right arrow Articles by Buchmeier, M. J.

 Previous Article  |  Next Article 

Journal of Virology, August 2006, p. 7918-7928, Vol. 80, No. 16
0022-538X/06/$08.00+0     doi:10.1128/JVI.00645-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Supramolecular Architecture of Severe Acute Respiratory Syndrome Coronavirus Revealed by Electron Cryomicroscopy{dagger}

Benjamin W. Neuman,1* Brian D. Adair,2 Craig Yoshioka,2 Joel D. Quispe,2 Gretchen Orca,2 Peter Kuhn,2 Ronald A. Milligan,2 Mark Yeager,2,3 and Michael J. Buchmeier1

Departments of Molecular and Integrative Neurosciences,1 Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, California 92037,2 Scripps Clinic, Department of Cardiovascular Diseases, 10666 N. Torrey Pines Rd., La Jolla, California 920373

Received 30 March 2006/ Accepted 30 May 2006

Coronavirus particles are enveloped and pleomorphic and are thus refractory to crystallization and symmetry-assisted reconstruction. A novel methodology of single-particle image analysis was applied to selected virus features to obtain a detailed model of the oligomeric state and spatial relationships among viral structural proteins. Two-dimensional images of the S, M, and N structural proteins of severe acute respiratory syndrome coronavirus and two other coronaviruses were refined to a resolution of ~4 nm. Proteins near the viral membrane were arranged in overlapping lattices surrounding a disordered core. Trimeric glycoprotein spikes were in register with four underlying ribonucleoprotein densities. However, the spikes were dispensable for ribonucleoprotein lattice formation. The ribonucleoprotein particles displayed coiled shapes when released from the viral membrane. Our results contribute to the understanding of the assembly pathway used by coronaviruses and other pleomorphic viruses and provide the first detailed view of coronavirus ultrastructure.


* Corresponding author. Mailing address: Department of Molecular and Integrative Neuroscience, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Phone: (858) 784-7162. Fax: (858) 784-7369. E-mail: bneuman{at}scripps.edu.

{dagger} This is TSRI manuscript 16733-NP.


Journal of Virology, August 2006, p. 7918-7928, Vol. 80, No. 16
0022-538X/06/$08.00+0     doi:10.1128/JVI.00645-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Hurst, K. R., Koetzner, C. A., Masters, P. S. (2009). Identification of In Vivo-Interacting Domains of the Murine Coronavirus Nucleocapsid Protein. J. Virol. 83: 7221-7234 [Abstract] [Full Text]  
  • Spilman, M. S., Welbon, C., Nelson, E., Dokland, T. (2009). Cryo-electron tomography of porcine reproductive and respiratory syndrome virus: organization of the nucleocapsid. J. Gen. Virol. 90: 527-535 [Abstract] [Full Text]  
  • Barcena, M., Oostergetel, G. T., Bartelink, W., Faas, F. G. A., Verkleij, A., Rottier, P. J. M., Koster, A. J., Bosch, B. J. (2009). Cryo-electron tomography of mouse hepatitis virus: Insights into the structure of the coronavirion. Proc. Natl. Acad. Sci. USA 106: 582-587 [Abstract] [Full Text]  
  • Neuman, B. W., Joseph, J. S., Saikatendu, K. S., Serrano, P., Chatterjee, A., Johnson, M. A., Liao, L., Klaus, J. P., Yates, J. R. III, Wuthrich, K., Stevens, R. C., Buchmeier, M. J., Kuhn, P. (2008). Proteomics Analysis Unravels the Functional Repertoire of Coronavirus Nonstructural Protein 3. J. Virol. 82: 5279-5294 [Abstract] [Full Text]  
  • Boscarino, J. A., Logan, H. L., Lacny, J. J., Gallagher, T. M. (2008). Envelope Protein Palmitoylations Are Crucial for Murine Coronavirus Assembly. J. Virol. 82: 2989-2999 [Abstract] [Full Text]  
  • Saikatendu, K. S., Joseph, J. S., Subramanian, V., Neuman, B. W., Buchmeier, M. J., Stevens, R. C., Kuhn, P. (2007). Ribonucleocapsid Formation of Severe Acute Respiratory Syndrome Coronavirus through Molecular Action of the N-Terminal Domain of N Protein. J. Virol. 81: 3913-3921 [Abstract] [Full Text]