Efficient assembly and release of SARS coronavirus-like particles by a heterologous expression system.
Identifieur interne : 005799 ( Main/Merge ); précédent : 005798; suivant : 005800Efficient assembly and release of SARS coronavirus-like particles by a heterologous expression system.
Auteurs : Eduardo Mortola [Royaume-Uni] ; Polly RoySource :
- FEBS letters [ 0014-5793 ] ; 2004.
Descripteurs français
- KwdFr :
- Animaux, Assemblage viral, Baculoviridae (génétique), Cellules cultivées, Cytométrie en flux, Protéines recombinantes (métabolisme), Spodoptera, Technique d'immunofluorescence indirecte, Technique de Western, Virion (isolement et purification), Virion (métabolisme), Virion (ultrastructure), Virus du SRAS (métabolisme), Électrophorèse sur gel de polyacrylamide.
- MESH :
- génétique : Baculoviridae.
- isolement et purification : Virion.
- métabolisme : Protéines recombinantes, Virion, Virus du SRAS.
- ultrastructure : Animaux, Assemblage viral, Cellules cultivées, Cytométrie en flux, Spodoptera, Technique d'immunofluorescence indirecte, Technique de Western, Virion, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Animals, Baculoviridae (genetics), Blotting, Western, Cells, Cultured, Electrophoresis, Polyacrylamide Gel, Flow Cytometry, Fluorescent Antibody Technique, Indirect, Recombinant Proteins (metabolism), SARS Virus (metabolism), Spodoptera, Virion (isolation & purification), Virion (metabolism), Virion (ultrastructure), Virus Assembly.
- MESH :
- chemical , metabolism : Recombinant Proteins.
- genetics : Baculoviridae.
- isolation & purification : Virion.
- metabolism : SARS Virus, Virion.
- ultrastructure : Virion.
- Animals, Blotting, Western, Cells, Cultured, Electrophoresis, Polyacrylamide Gel, Flow Cytometry, Fluorescent Antibody Technique, Indirect, Spodoptera, Virus Assembly.
Abstract
Virus-like particles (VLPs) produced by recombinant expression of the major viral structural proteins could be an attractive method for severe acute respiratory syndrome (SARS) control. In this study, using the baculovirus system, we generated recombinant viruses that expressed S, E, M and N structural proteins of SARS-CoV either individually or simultaneously. The expression level, size and authenticity of each recombinant SARS-CoV protein were determined. In addition, immunofluorescence and FACS analysis confirmed the cell surface expression of the S protein. Co-infections of insect cells with two recombinant viruses demonstrated that M and E could assemble readily to form smooth surfaced VLPs. On the other hand, simultaneous high level expression of S, E and M by a single recombinant virus allowed the very efficient assembly and release of VLPs. These data demonstrate that the VLPs are morphological mimics of virion particles. The high level expression of VLPs with correct S protein conformation by a single recombinant baculovirus offers a potential candidate vaccine for SARS.
DOI: 10.1016/j.febslet.2004.09.009
PubMed: 15474033
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pubmed:15474033Le document en format XML
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Western</term><term>Virion (isolement et purification)</term><term>Virion (métabolisme)</term><term>Virion (ultrastructure)</term><term>Virus du SRAS (métabolisme)</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Baculoviridae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Baculoviridae</term></keywords><keywords scheme="MESH" qualifier="isolation & purification" xml:lang="en"><term>Virion</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Virion</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term><term>Virion</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines recombinantes</term><term>Virion</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Virion</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Blotting, Western</term><term>Cells, Cultured</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Flow Cytometry</term><term>Fluorescent Antibody Technique, Indirect</term><term>Spodoptera</term><term>Virus Assembly</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Animaux</term><term>Assemblage viral</term><term>Cellules cultivées</term><term>Cytométrie en flux</term><term>Spodoptera</term><term>Technique d'immunofluorescence indirecte</term><term>Technique de Western</term><term>Virion</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Virus-like particles (VLPs) produced by recombinant expression of the major viral structural proteins could be an attractive method for severe acute respiratory syndrome (SARS) control. In this study, using the baculovirus system, we generated recombinant viruses that expressed S, E, M and N structural proteins of SARS-CoV either individually or simultaneously. The expression level, size and authenticity of each recombinant SARS-CoV protein were determined. In addition, immunofluorescence and FACS analysis confirmed the cell surface expression of the S protein. Co-infections of insect cells with two recombinant viruses demonstrated that M and E could assemble readily to form smooth surfaced VLPs. On the other hand, simultaneous high level expression of S, E and M by a single recombinant virus allowed the very efficient assembly and release of VLPs. These data demonstrate that the VLPs are morphological mimics of virion particles. The high level expression of VLPs with correct S protein conformation by a single recombinant baculovirus offers a potential candidate vaccine for SARS.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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