Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy.
Identifieur interne : 003C84 ( Main/Exploration ); précédent : 003C83; suivant : 003C85Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy.
Auteurs : Benjamin W. Neuman [États-Unis] ; Brian D. Adair ; Craig Yoshioka ; Joel D. Quispe ; Gretchen Orca ; Peter Kuhn ; Ronald A. Milligan ; Mark Yeager ; Michael J. BuchmeierSource :
- Journal of virology [ 0022-538X ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
- ultrastructure : Cryomicroscopie électronique, Protéines virales structurales, Ribonucléoprotéines, Virus du SRAS.
English descriptors
- KwdEn :
- MESH :
- chemical , ultrastructure : Ribonucleoproteins, Viral Structural Proteins.
- ultrastructure : SARS Virus.
- Cryoelectron Microscopy.
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.
DOI: 10.1128/JVI.00645-06
PubMed: 16873249
Affiliations:
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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.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><noCountry><name sortKey="Adair, Brian D" sort="Adair, Brian D" uniqKey="Adair B" first="Brian D" last="Adair">Brian D. Adair</name><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J" last="Buchmeier">Michael J. Buchmeier</name><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name><name sortKey="Milligan, Ronald A" sort="Milligan, Ronald A" uniqKey="Milligan R" first="Ronald A" last="Milligan">Ronald A. 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