SrasV1, PascalFrancis, Corpus, bibRecord, 000245

The M, E, and N Structural Proteins of the Severe Acute Respiratory Syndrome Coronavirus Are Required for Efficient Assembly, Trafficking, and Release of Virus-Like Particles

Identifieur interne : 000245 ( PascalFrancis/Corpus ); précédent : 000244; suivant : 000246

The M, E, and N Structural Proteins of the Severe Acute Respiratory Syndrome Coronavirus Are Required for Efficient Assembly, Trafficking, and Release of Virus-Like Particles

Auteurs : Y. L. Siu ; K. T. Teoh ; J. Lo ; C. M. Chan ; F. Kien ; N. Escriou ; S. W. Tsao ; J. M. Nicholls ; R. Altmeyer ; J. S. M. Peiris ; R. Bruzzone ; B. Nal

Source :

Journal of virology [ 0022-538X ] ; 2008.

RBID : Pascal:08-0522049

Descripteurs français

Pascal (Inist)
- Coronavirus, Protéine, Libération, Particule type viral, Virologie, Syndrome respiratoire aigu sévère.

English descriptors

KwdEn :
- Coronavirus, Protein, Release, Severe acute respiratory syndrome, Virology, Virus like particle.

Abstract

The production of virus-like particles (VLPs) constitutes a relevant and safe model to study molecular determinants of virion egress. The minimal requirement for the assembly of VLPs for the coronavirus responsible for severe acute respiratory syndrome in humans (SARS-CoV) is still controversial. Recent studies have shown that SARS-CoV VLP formation depends on either M and E proteins or M and N proteins. Here we show that both E and N proteins must be coexpressed with M protein for the efficient production and release of VLPs by transfected Vero E6 cells. This suggests that the mechanism of SARS-CoV assembly differs from that of other studied coronaviruses, which only require M and E proteins for VLP formation. When coexpressed, the native envelope trimeric S glycoprotein is incorporated onto VLPs. Interestingly, when a fluorescent protein tag is added to the C-terminal end of N or S protein, but not M protein, the chimeric viral proteins can be assembled within VLPs and allow visualization of VLP production and trafficking in living cells by state-of-the-art imaging technologies. Fluorescent VLPs will be used further to investigate the role of cellular machineries during SARS-CoV egress.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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Format Inist (serveur)

NO :	PASCAL 08-0522049 INIST
ET :	The M, E, and N Structural Proteins of the Severe Acute Respiratory Syndrome Coronavirus Are Required for Efficient Assembly, Trafficking, and Release of Virus-Like Particles
AU :	SIU (Y. L.); TEOH (K. T.); LO (J.); CHAN (C. M.); KIEN (F.); ESCRIOU (N.); TSAO (S. W.); NICHOLLS (J. M.); ALTMEYER (R.); PEIRIS (J. S. M.); BRUZZONE (R.); NAL (B.)
AF :	HKU-Pasteur Research Centre, 8 Sassoon Road/Hong-Kong (1 aut., 2 aut., 5 aut., 10 aut., 11 aut., 12 aut.); Department of Pathology, The University of Hong Kong, Queen Mary Hospital/Hong-Kong (3 aut., 8 aut.); Department of Microbiology, The University of Hong Kong, 21 Sassoon Road/Hong-Kong (4 aut., 10 aut.); Institut Pasteur, Unité de Génétique Moléculaire des Virus Respiratoires, URA-CNRS 3015, 25-28 Rue du Docteur Roux/75724 Paris/France (6 aut.); Department of Anatomy, The University of Hong Kong, 21 Sassoon Road/Hong-Kong (7 aut.); CombinatoRx-Singapore Pte, Ltd., 11 Biopolis Way/138667 Singapore/Singapour (9 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2008; Vol. 82; No. 22; Pp. 11318-11330; Bibl. 70 ref.
LA :	Anglais
EA :	The production of virus-like particles (VLPs) constitutes a relevant and safe model to study molecular determinants of virion egress. The minimal requirement for the assembly of VLPs for the coronavirus responsible for severe acute respiratory syndrome in humans (SARS-CoV) is still controversial. Recent studies have shown that SARS-CoV VLP formation depends on either M and E proteins or M and N proteins. Here we show that both E and N proteins must be coexpressed with M protein for the efficient production and release of VLPs by transfected Vero E6 cells. This suggests that the mechanism of SARS-CoV assembly differs from that of other studied coronaviruses, which only require M and E proteins for VLP formation. When coexpressed, the native envelope trimeric S glycoprotein is incorporated onto VLPs. Interestingly, when a fluorescent protein tag is added to the C-terminal end of N or S protein, but not M protein, the chimeric viral proteins can be assembled within VLPs and allow visualization of VLP production and trafficking in living cells by state-of-the-art imaging technologies. Fluorescent VLPs will be used further to investigate the role of cellular machineries during SARS-CoV egress.
CC :	002A05C10
FD :	Coronavirus; Protéine; Libération; Particule type viral; Virologie; Syndrome respiratoire aigu sévère
FG :	Coronaviridae; Nidovirales; Virus; Pathologie de l'appareil respiratoire; Virose; Infection; Pathologie des poumons
ED :	Coronavirus; Protein; Release; Virus like particle; Virology; Severe acute respiratory syndrome
EG :	Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease
SD :	Coronavirus; Proteína; Liberación; Partícula tipo vírico; Virología; Síndrome respiratorio agudo severo
LO :	INIST-13592.354000184310400320
ID :	08-0522049

Links to Exploration step

Pascal:08-0522049

Le document en format XML

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<author><name sortKey="Nicholls, J M" sort="Nicholls, J M" uniqKey="Nicholls J" first="J. M." last="Nicholls">J. M. Nicholls</name>
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<author><name sortKey="Altmeyer, R" sort="Altmeyer, R" uniqKey="Altmeyer R" first="R." last="Altmeyer">R. Altmeyer</name>
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<author><name sortKey="Peiris, J S M" sort="Peiris, J S M" uniqKey="Peiris J" first="J. S. M." last="Peiris">J. S. M. Peiris</name>
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<author><name sortKey="Bruzzone, R" sort="Bruzzone, R" uniqKey="Bruzzone R" first="R." last="Bruzzone">R. Bruzzone</name>
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<author><name sortKey="Nal, B" sort="Nal, B" uniqKey="Nal B" first="B." last="Nal">B. Nal</name>
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<front><div type="abstract" xml:lang="en">The production of virus-like particles (VLPs) constitutes a relevant and safe model to study molecular determinants of virion egress. The minimal requirement for the assembly of VLPs for the coronavirus responsible for severe acute respiratory syndrome in humans (SARS-CoV) is still controversial. Recent studies have shown that SARS-CoV VLP formation depends on either M and E proteins or M and N proteins. Here we show that both E and N proteins must be coexpressed with M protein for the efficient production and release of VLPs by transfected Vero E6 cells. This suggests that the mechanism of SARS-CoV assembly differs from that of other studied coronaviruses, which only require M and E proteins for VLP formation. When coexpressed, the native envelope trimeric S glycoprotein is incorporated onto VLPs. Interestingly, when a fluorescent protein tag is added to the C-terminal end of N or S protein, but not M protein, the chimeric viral proteins can be assembled within VLPs and allow visualization of VLP production and trafficking in living cells by state-of-the-art imaging technologies. Fluorescent VLPs will be used further to investigate the role of cellular machineries during SARS-CoV egress.</div>
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<fA08 i1="01" i2="1" l="ENG"><s1>The M, E, and N Structural Proteins of the Severe Acute Respiratory Syndrome Coronavirus Are Required for Efficient Assembly, Trafficking, and Release of Virus-Like Particles</s1>
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<sZ>10 aut.</sZ>
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<fA14 i1="02"><s1>Department of Pathology, The University of Hong Kong, Queen Mary Hospital</s1>
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<fA14 i1="03"><s1>Department of Microbiology, The University of Hong Kong, 21 Sassoon Road</s1>
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<fA14 i1="05"><s1>Department of Anatomy, The University of Hong Kong, 21 Sassoon Road</s1>
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</fA14>
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<ET>The M, E, and N Structural Proteins of the Severe Acute Respiratory Syndrome Coronavirus Are Required for Efficient Assembly, Trafficking, and Release of Virus-Like Particles</ET>
<AU>SIU (Y. L.); TEOH (K. T.); LO (J.); CHAN (C. M.); KIEN (F.); ESCRIOU (N.); TSAO (S. W.); NICHOLLS (J. M.); ALTMEYER (R.); PEIRIS (J. S. M.); BRUZZONE (R.); NAL (B.)</AU>
<AF>HKU-Pasteur Research Centre, 8 Sassoon Road/Hong-Kong (1 aut., 2 aut., 5 aut., 10 aut., 11 aut., 12 aut.); Department of Pathology, The University of Hong Kong, Queen Mary Hospital/Hong-Kong (3 aut., 8 aut.); Department of Microbiology, The University of Hong Kong, 21 Sassoon Road/Hong-Kong (4 aut., 10 aut.); Institut Pasteur, Unité de Génétique Moléculaire des Virus Respiratoires, URA-CNRS 3015, 25-28 Rue du Docteur Roux/75724 Paris/France (6 aut.); Department of Anatomy, The University of Hong Kong, 21 Sassoon Road/Hong-Kong (7 aut.); CombinatoRx-Singapore Pte, Ltd., 11 Biopolis Way/138667 Singapore/Singapour (9 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
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<EA>The production of virus-like particles (VLPs) constitutes a relevant and safe model to study molecular determinants of virion egress. The minimal requirement for the assembly of VLPs for the coronavirus responsible for severe acute respiratory syndrome in humans (SARS-CoV) is still controversial. Recent studies have shown that SARS-CoV VLP formation depends on either M and E proteins or M and N proteins. Here we show that both E and N proteins must be coexpressed with M protein for the efficient production and release of VLPs by transfected Vero E6 cells. This suggests that the mechanism of SARS-CoV assembly differs from that of other studied coronaviruses, which only require M and E proteins for VLP formation. When coexpressed, the native envelope trimeric S glycoprotein is incorporated onto VLPs. Interestingly, when a fluorescent protein tag is added to the C-terminal end of N or S protein, but not M protein, the chimeric viral proteins can be assembled within VLPs and allow visualization of VLP production and trafficking in living cells by state-of-the-art imaging technologies. Fluorescent VLPs will be used further to investigate the role of cellular machineries during SARS-CoV egress.</EA>
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The M, E, and N Structural Proteins of the Severe Acute Respiratory Syndrome Coronavirus Are Required for Efficient Assembly, Trafficking, and Release of Virus-Like Particles

The M, E, and N Structural Proteins of the Severe Acute Respiratory Syndrome Coronavirus Are Required for Efficient Assembly, Trafficking, and Release of Virus-Like Particles

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