SrasV1, Ncbi, Merge, bibRecord, 000984

A single amino acid mutation in the spike protein of coronavirus infectious bronchitis virus hampers its maturation and incorporation into virions at the nonpermissive temperature.

Identifieur interne : 000984 ( Ncbi/Merge ); précédent : 000983; suivant : 000985

A single amino acid mutation in the spike protein of coronavirus infectious bronchitis virus hampers its maturation and incorporation into virions at the nonpermissive temperature.

Auteurs : S. Shen [Singapour] ; Y C Law ; D X Liu

Source :

Virology [ 0042-6822 ] ; 2004.

RBID : pubmed:15302214

Descripteurs français

English descriptors

KwdEn :
- Acclimatization, Amino Acid Substitution, Animals, Chlorocebus aethiops, Cytoplasm (metabolism), Glutamine (chemistry), Glycoside Hydrolases, HeLa Cells, Humans, Infectious bronchitis virus (genetics), Infectious bronchitis virus (physiology), Leucine (chemistry), Membrane Glycoproteins (biosynthesis), Membrane Glycoproteins (genetics), Membrane Glycoproteins (physiology), Point Mutation, Spike Glycoprotein, Coronavirus, Temperature, Transfection, Vero Cells, Viral Envelope Proteins (biosynthesis), Viral Envelope Proteins (genetics), Viral Envelope Proteins (physiology), Virus Assembly.
MESH :
- chemical , biosynthesis : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , chemistry : Glutamine, Leucine.
- genetics : Infectious bronchitis virus, Membrane Glycoproteins, Viral Envelope Proteins.
- metabolism : Cytoplasm.
- physiology : Infectious bronchitis virus, Membrane Glycoproteins, Viral Envelope Proteins.
- Acclimatization, Amino Acid Substitution, Animals, Chlorocebus aethiops, Glycoside Hydrolases, HeLa Cells, Humans, Point Mutation, Spike Glycoprotein, Coronavirus, Temperature, Transfection, Vero Cells, Virus Assembly.

Abstract

The spike (S) glycoprotein of coronavirus is responsible for receptor binding and membrane fusion. A number of variants with deletions and mutations in the S protein have been isolated from naturally and persistently infected animals and tissue cultures. Here, we report the emergence and isolation of two temperature sensitive (ts) mutants and a revertant in the process of cold-adaptation of coronavirus infectious bronchitis virus (IBV) to a monkey kidney cell line. The complete sequences of wild type (wt) virus, two ts mutants, and the revertant were compared and variations linked to phenotypes were mapped. A single amino acid reversion (L294-to-Q) in the S protein is sufficient to abrogate the ts phenotype. Interestingly, unlike wt virus, the revertant grows well at and below 32 degrees C, the permissive temperature, as it carries other mutations in multiple genes that might be associated with the cold-adaptation phenotype. If the two ts mutants were allowed to enter cells at 32 degrees C, the S protein was synthesized, core-glycosylated and at least partially modified at 40 degrees C. However, compared with wt virus and the revertant, no infectious particles of these ts mutants were assembled and released from the ts mutant-infected cells at 40 degrees C. Evidence presented demonstrated that the Q294-to-L294 mutation, located at a highly conserved domain of the S1 subunit, might hamper processing of the S protein to a matured 180-kDa, endo-glycosidase H-resistant glycoprotein and the translocation of the protein to the cell surface. Consequently, some essential functions of the S protein, including mediation of cell-to-cell fusion and its incorporation into virions, were completely abolished.

DOI: 10.1016/j.virol.2004.06.016
PubMed: 15302214

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pubmed:15302214

Le document en format XML

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<term>Cytoplasm (metabolism)</term>
<term>Glutamine (chemistry)</term>
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<term>HeLa Cells</term>
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<term>Infectious bronchitis virus (physiology)</term>
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<term>Vero Cells</term>
<term>Viral Envelope Proteins (biosynthesis)</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Envelope Proteins (physiology)</term>
<term>Virus Assembly</term>
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<term>Animaux</term>
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<term>Cellules Vero</term>
<term>Cytoplasme (métabolisme)</term>
<term>Glutamine ()</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires (biosynthèse)</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (physiologie)</term>
<term>Glycosidases</term>
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<term>Leucine ()</term>
<term>Mutation ponctuelle</term>
<term>Protéines de l'enveloppe virale (biosynthèse)</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (physiologie)</term>
<term>Substitution d'acide aminé</term>
<term>Température</term>
<term>Transfection</term>
<term>Virus de la bronchite infectieuse (génétique)</term>
<term>Virus de la bronchite infectieuse (physiologie)</term>
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<term>Leucine</term>
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<term>Protéines de l'enveloppe virale</term>
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<term>Viral Envelope Proteins</term>
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<term>Protéines de l'enveloppe virale</term>
<term>Virus de la bronchite infectieuse</term>
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<term>Viral Envelope Proteins</term>
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<term>Animals</term>
<term>Chlorocebus aethiops</term>
<term>Glycoside Hydrolases</term>
<term>HeLa Cells</term>
<term>Humans</term>
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<term>Vero Cells</term>
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<term>Cellules HeLa</term>
<term>Cellules Vero</term>
<term>Glutamine</term>
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<term>Humains</term>
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<front><div type="abstract" xml:lang="en">The spike (S) glycoprotein of coronavirus is responsible for receptor binding and membrane fusion. A number of variants with deletions and mutations in the S protein have been isolated from naturally and persistently infected animals and tissue cultures. Here, we report the emergence and isolation of two temperature sensitive (ts) mutants and a revertant in the process of cold-adaptation of coronavirus infectious bronchitis virus (IBV) to a monkey kidney cell line. The complete sequences of wild type (wt) virus, two ts mutants, and the revertant were compared and variations linked to phenotypes were mapped. A single amino acid reversion (L294-to-Q) in the S protein is sufficient to abrogate the ts phenotype. Interestingly, unlike wt virus, the revertant grows well at and below 32 degrees C, the permissive temperature, as it carries other mutations in multiple genes that might be associated with the cold-adaptation phenotype. If the two ts mutants were allowed to enter cells at 32 degrees C, the S protein was synthesized, core-glycosylated and at least partially modified at 40 degrees C. However, compared with wt virus and the revertant, no infectious particles of these ts mutants were assembled and released from the ts mutant-infected cells at 40 degrees C. Evidence presented demonstrated that the Q294-to-L294 mutation, located at a highly conserved domain of the S1 subunit, might hamper processing of the S protein to a matured 180-kDa, endo-glycosidase H-resistant glycoprotein and the translocation of the protein to the cell surface. Consequently, some essential functions of the S protein, including mediation of cell-to-cell fusion and its incorporation into virions, were completely abolished.</div>
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<Abstract><AbstractText>The spike (S) glycoprotein of coronavirus is responsible for receptor binding and membrane fusion. A number of variants with deletions and mutations in the S protein have been isolated from naturally and persistently infected animals and tissue cultures. Here, we report the emergence and isolation of two temperature sensitive (ts) mutants and a revertant in the process of cold-adaptation of coronavirus infectious bronchitis virus (IBV) to a monkey kidney cell line. The complete sequences of wild type (wt) virus, two ts mutants, and the revertant were compared and variations linked to phenotypes were mapped. A single amino acid reversion (L294-to-Q) in the S protein is sufficient to abrogate the ts phenotype. Interestingly, unlike wt virus, the revertant grows well at and below 32 degrees C, the permissive temperature, as it carries other mutations in multiple genes that might be associated with the cold-adaptation phenotype. If the two ts mutants were allowed to enter cells at 32 degrees C, the S protein was synthesized, core-glycosylated and at least partially modified at 40 degrees C. However, compared with wt virus and the revertant, no infectious particles of these ts mutants were assembled and released from the ts mutant-infected cells at 40 degrees C. Evidence presented demonstrated that the Q294-to-L294 mutation, located at a highly conserved domain of the S1 subunit, might hamper processing of the S protein to a matured 180-kDa, endo-glycosidase H-resistant glycoprotein and the translocation of the protein to the cell surface. Consequently, some essential functions of the S protein, including mediation of cell-to-cell fusion and its incorporation into virions, were completely abolished.</AbstractText>
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A single amino acid mutation in the spike protein of coronavirus infectious bronchitis virus hampers its maturation and incorporation into virions at the nonpermissive temperature.

A single amino acid mutation in the spike protein of coronavirus infectious bronchitis virus hampers its maturation and incorporation into virions at the nonpermissive temperature.

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