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Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron ciyomicroscopy

Academic Article
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Overview

related to degree

  • Yoshioka, Craig, Ph.D. in Biophysics, Scripps Research 2003 - 2008

authors

  • Neuman, B. W.
  • Adair, B. D.
  • Yoshioka, Craig
  • Quispe, J. D.
  • Orca, G.
  • Kuhn, Peter
  • Milligan, Ronald
  • Yeager, Mark
  • Buchmeier, M. J.

publication date

  • August 2006

journal

  • Journal of Virology  Journal

abstract

  • 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 approximately 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.

subject areas

  • Cryoelectron Microscopy
  • Ribonucleoproteins
  • SARS Virus
  • Viral Structural Proteins
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Identity

PubMed Central ID

  • PMC1563832

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.00645-06

PubMed ID

  • 16873249
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Additional Document Info

start page

  • 7918

end page

  • 7928

volume

  • 80

issue

  • 16

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