SrasV1, Main, Exploration, bibRecord, 001895

Negatively charged residues in the endodomain are critical for specific assembly of spike protein into murine coronavirus.

Identifieur interne : 001895 ( Main/Exploration ); précédent : 001894; suivant : 001896

Negatively charged residues in the endodomain are critical for specific assembly of spike protein into murine coronavirus.

Auteurs : Qianqian Yao [République populaire de Chine] ; Paul S. Masters ; Rong Ye

Source :

Virology [ 1096-0341 ] ; 2013.

RBID : pubmed:23628137

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Cattle, Cell Line, Coronavirus, Bovine (genetics), Coronavirus, Bovine (metabolism), Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Mice, Molecular Sequence Data, Murine hepatitis virus (chemistry), Murine hepatitis virus (genetics), Murine hepatitis virus (metabolism), Mutation, Protein Structure, Tertiary (genetics), SARS Virus, Spike Glycoprotein, Coronavirus, Transmissible gastroenteritis virus (genetics), Transmissible gastroenteritis virus (metabolism), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virus Assembly.
MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemistry : Murine hepatitis virus.
- genetics : Coronavirus, Bovine, Membrane Glycoproteins, Murine hepatitis virus, Protein Structure, Tertiary, Transmissible gastroenteritis virus, Viral Envelope Proteins.
- metabolism : Coronavirus, Bovine, Membrane Glycoproteins, Murine hepatitis virus, Transmissible gastroenteritis virus, Viral Envelope Proteins.
- Amino Acid Sequence, Animals, Cattle, Cell Line, Humans, Mice, Molecular Sequence Data, Mutation, SARS Virus, Spike Glycoprotein, Coronavirus, Virus Assembly.

Abstract

Coronavirus spike (S) protein assembles into virions via its carboxy-terminus, which is composed of a transmembrane domain and an endodomain. Here, the carboxy-terminal charge-rich motif in the endodomain was verified to be critical for the specificity of S assembly into mouse hepatitis virus (MHV). Recombinant MHVs exhibited a range of abilities to accommodate the homologous S endodomains from the betacoronaviruses bovine coronavirus and human SARS-associated coronavirus, the alphacoronavirus porcine transmissible gastroenteritis virus (TGEV), and the gammacoronavirus avian infectious bronchitis virus respectively. Interestingly, in TGEV endodomain chimeras the reverting mutations resulted in stronger S incorporation into virions, and a net gain of negatively charged residues in the charge-rich motif accounted for the improvement. Additionally, MHV S assembly could also be rescued by the acidic carboxy-terminal domain of the nucleocapsid protein. These results indicate an important role for negatively charged endodomain residues in the incorporation of MHV S protein into assembled virions.

DOI: 10.1016/j.virol.2013.04.001
PubMed: 23628137

Affiliations:

République populaire de Chine

Le document en format XML

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<term>Coronavirus, Bovine (metabolism)</term>
<term>Humans</term>
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<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (metabolism)</term>
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<term>Murine hepatitis virus (genetics)</term>
<term>Murine hepatitis virus (metabolism)</term>
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<term>Protein Structure, Tertiary (genetics)</term>
<term>SARS Virus</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Transmissible gastroenteritis virus (genetics)</term>
<term>Transmissible gastroenteritis virus (metabolism)</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Envelope Proteins (metabolism)</term>
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<term>Coronavirus bovin (génétique)</term>
<term>Coronavirus bovin (métabolisme)</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
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<term>Lignée cellulaire</term>
<term>Mutation</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
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<term>Virus de la gastroentérite transmissible (métabolisme)</term>
<term>Virus du SRAS</term>
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<term>Membrane Glycoproteins</term>
<term>Murine hepatitis virus</term>
<term>Protein Structure, Tertiary</term>
<term>Transmissible gastroenteritis virus</term>
<term>Viral Envelope Proteins</term>
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<term>Glycoprotéines membranaires</term>
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<term>Structure tertiaire des protéines</term>
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<term>Virus de la gastroentérite transmissible</term>
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<term>Cattle</term>
<term>Cell Line</term>
<term>Humans</term>
<term>Mice</term>
<term>Molecular Sequence Data</term>
<term>Mutation</term>
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<front><div type="abstract" xml:lang="en">Coronavirus spike (S) protein assembles into virions via its carboxy-terminus, which is composed of a transmembrane domain and an endodomain. Here, the carboxy-terminal charge-rich motif in the endodomain was verified to be critical for the specificity of S assembly into mouse hepatitis virus (MHV). Recombinant MHVs exhibited a range of abilities to accommodate the homologous S endodomains from the betacoronaviruses bovine coronavirus and human SARS-associated coronavirus, the alphacoronavirus porcine transmissible gastroenteritis virus (TGEV), and the gammacoronavirus avian infectious bronchitis virus respectively. Interestingly, in TGEV endodomain chimeras the reverting mutations resulted in stronger S incorporation into virions, and a net gain of negatively charged residues in the charge-rich motif accounted for the improvement. Additionally, MHV S assembly could also be rescued by the acidic carboxy-terminal domain of the nucleocapsid protein. These results indicate an important role for negatively charged endodomain residues in the incorporation of MHV S protein into assembled virions.</div>
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Negatively charged residues in the endodomain are critical for specific assembly of spike protein into murine coronavirus.

Negatively charged residues in the endodomain are critical for specific assembly of spike protein into murine coronavirus.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

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