Structure of Correctly Self-Assembled Bluetongue Virus-like Particles
Identifieur interne : 001A24 ( Istex/Checkpoint ); précédent : 001A23; suivant : 001A25Structure of Correctly Self-Assembled Bluetongue Virus-like Particles
Auteurs : Elizabeth A. Hewat [États-Unis] ; Timothy F. Booth [États-Unis] ; Polly Roy [États-Unis]Source :
- Journal of Structural Biology [ 1047-8477 ] ; 1994.
Abstract
Abstract: Bluetongue virus-like particles (VLPs), synthesized by coexpression of VP2, VP3, VP5, and VP7 using recombinant baculoviruses, have been examined by cryoelectron microscopy and image analysis. The 3-D reconstruction of these VLPs reveals an icosahedral structure 86 nm in diameter with essentially the same features as for the native Bluetongue virus (BTV) particle. The VLP is thus shown to contain the four constituent proteins as the native virus particle, with each of the protein positions highly occupied. Since the BTV core-like particle formed by coexpression of VP3 and VP7 lacks five VP7 trimers around each of the five-fold axes, it appears that the presence of the outer capsid proteins VP2 and VP5 is necessary for the adhesion of these VP7 trimers around the five-fold axes. The observed spontaneous formation of complete VLP in the absence of the BTV nonstructural proteins implies that the nonstructural proteins are not necessary for the formation of the double-shelled viral capsid. However, the nonstructural proteins may be involved in different aspects of genome replication and packaging.
Url:
DOI: 10.1006/jsbi.1994.1019
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Hewat</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Alabama</region></placeName><wicri:cityArea>Institut de Biologie Structurale, 41 Avenue des Martyrs, 38027 Grenoble Cedex 1, France; NERC Institute of Virology and Environmental Microbiology, Mansfield Road, Oxford OX1 3SR, United Kingdom; Laboratory of Molecular Biophysics, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom; and Department of Environmental Health Sciences, School of Public Health, The University of Alabama at Birmingham, University Station, Birmingham</wicri:cityArea></affiliation></author><author><name sortKey="Booth, Timothy F" sort="Booth, Timothy F" uniqKey="Booth T" first="Timothy F." last="Booth">Timothy F. Booth</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Alabama</region></placeName><wicri:cityArea>Institut de Biologie Structurale, 41 Avenue des Martyrs, 38027 Grenoble Cedex 1, France; NERC Institute of Virology and Environmental Microbiology, Mansfield Road, Oxford OX1 3SR, United Kingdom; Laboratory of Molecular Biophysics, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom; and Department of Environmental Health Sciences, School of Public Health, The University of Alabama at Birmingham, University Station, Birmingham</wicri:cityArea></affiliation></author><author><name sortKey="Roy, Polly" sort="Roy, Polly" uniqKey="Roy P" first="Polly" last="Roy">Polly Roy</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Alabama</region></placeName><wicri:cityArea>Institut de Biologie Structurale, 41 Avenue des Martyrs, 38027 Grenoble Cedex 1, France; NERC Institute of Virology and Environmental Microbiology, Mansfield Road, Oxford OX1 3SR, United Kingdom; Laboratory of Molecular Biophysics, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom; and Department of Environmental Health Sciences, School of Public Health, The University of Alabama at Birmingham, University Station, Birmingham</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Structural Biology</title><title level="j" type="abbrev">YJSBI</title><idno type="ISSN">1047-8477</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994">1994</date><biblScope unit="volume">112</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="183">183</biblScope><biblScope unit="page" to="191">191</biblScope></imprint><idno type="ISSN">1047-8477</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1047-8477</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Bluetongue virus-like particles (VLPs), synthesized by coexpression of VP2, VP3, VP5, and VP7 using recombinant baculoviruses, have been examined by cryoelectron microscopy and image analysis. The 3-D reconstruction of these VLPs reveals an icosahedral structure 86 nm in diameter with essentially the same features as for the native Bluetongue virus (BTV) particle. The VLP is thus shown to contain the four constituent proteins as the native virus particle, with each of the protein positions highly occupied. Since the BTV core-like particle formed by coexpression of VP3 and VP7 lacks five VP7 trimers around each of the five-fold axes, it appears that the presence of the outer capsid proteins VP2 and VP5 is necessary for the adhesion of these VP7 trimers around the five-fold axes. The observed spontaneous formation of complete VLP in the absence of the BTV nonstructural proteins implies that the nonstructural proteins are not necessary for the formation of the double-shelled viral capsid. However, the nonstructural proteins may be involved in different aspects of genome replication and packaging.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Alabama</li></region></list><tree><country name="États-Unis"><region name="Alabama"><name sortKey="Hewat, Elizabeth A" sort="Hewat, Elizabeth A" uniqKey="Hewat E" first="Elizabeth A." last="Hewat">Elizabeth A. Hewat</name></region><name sortKey="Booth, Timothy F" sort="Booth, Timothy F" uniqKey="Booth T" first="Timothy F." last="Booth">Timothy F. Booth</name><name sortKey="Roy, Polly" sort="Roy, Polly" uniqKey="Roy P" first="Polly" last="Roy">Polly Roy</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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