SrasV1, PubMed, Curation, bibRecord, 002149

The human severe acute respiratory syndrome coronavirus (SARS-CoV) 8b protein is distinct from its counterpart in animal SARS-CoV and down-regulates the expression of the envelope protein in infected cells.

Identifieur interne : 002149 ( PubMed/Curation ); précédent : 002148; suivant : 002150

The human severe acute respiratory syndrome coronavirus (SARS-CoV) 8b protein is distinct from its counterpart in animal SARS-CoV and down-regulates the expression of the envelope protein in infected cells.

Auteurs : Choong-Tat Keng ; Yook-Wah Choi ; Matthijs R A. Welkers ; Daphne Z L. Chan ; Shuo Shen ; Seng Gee Lim ; Wanjin Hong ; Yee-Joo Tan

Source :

Virology [ 0042-6822 ] ; 2006.

RBID : pubmed:16876844

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Blotting, Western, Cell Line, Cell Nucleus (chemistry), Chlorocebus aethiops, Cytoplasm (chemistry), Gene Expression Regulation, Viral, Humans, Immunoprecipitation, Microscopy, Fluorescence, Molecular Sequence Data, Protein Binding, RNA, Messenger (analysis), RNA, Messenger (genetics), RNA, Viral (analysis), RNA, Viral (genetics), Reverse Transcriptase Polymerase Chain Reaction, SARS Virus (genetics), SARS Virus (physiology), Transcription, Genetic, Viral Envelope Proteins (analysis), Viral Envelope Proteins (biosynthesis), Viral Matrix Proteins (analysis), Viral Matrix Proteins (genetics), Viral Matrix Proteins (physiology), Viral Proteins (analysis), Viral Proteins (genetics), Viral Proteins (physiology).
MESH :
- chemical , analysis : RNA, Messenger, RNA, Viral, Viral Envelope Proteins, Viral Matrix Proteins, Viral Proteins.
- chemical , biosynthesis : Viral Envelope Proteins.
- chemistry : Cell Nucleus, Cytoplasm.
- chemical , genetics : RNA, Messenger, RNA, Viral, SARS Virus, Viral Matrix Proteins, Viral Proteins.
- physiology : SARS Virus, Viral Matrix Proteins, Viral Proteins.
- Amino Acid Sequence, Animals, Blotting, Western, Cell Line, Chlorocebus aethiops, Gene Expression Regulation, Viral, Humans, Immunoprecipitation, Microscopy, Fluorescence, Molecular Sequence Data, Protein Binding, Reverse Transcriptase Polymerase Chain Reaction, Transcription, Genetic.

Abstract

The severe acute respiratory syndrome coronavirus (SARS-CoV), isolated from humans infected during the peak of epidemic, encodes two accessory proteins termed as 8a and 8b. Interestingly, the SARS-CoV isolated from animals contains an extra 29-nucleotide in this region such that these proteins are fused to become a single protein, 8ab. Here, we compared the cellular properties of the 8a, 8b and 8ab proteins by examining their cellular localizations and their abilities to interact with other SARS-CoV proteins. These results may suggest that the conformations of 8a and 8b are different from 8ab although nearly all the amino acids in 8a and 8b are found in 8ab. In addition, the expression of the structural protein, envelope (E), was down-regulated by 8b but not 8a or 8ab. Consequently, E was not detectable in SARS-CoV-infected cells that were expressing high levels of 8b. These findings suggest that 8b may modulate viral replication and/or pathogenesis.

DOI: 10.1016/j.virol.2006.06.026
PubMed: 16876844

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Choong-Tat Keng

<affiliation><nlm:affiliation>Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore, 138673.</nlm:affiliation>
<wicri:noCountry code="subField">138673</wicri:noCountry>
</affiliation>

Le document en format XML

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<front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV), isolated from humans infected during the peak of epidemic, encodes two accessory proteins termed as 8a and 8b. Interestingly, the SARS-CoV isolated from animals contains an extra 29-nucleotide in this region such that these proteins are fused to become a single protein, 8ab. Here, we compared the cellular properties of the 8a, 8b and 8ab proteins by examining their cellular localizations and their abilities to interact with other SARS-CoV proteins. These results may suggest that the conformations of 8a and 8b are different from 8ab although nearly all the amino acids in 8a and 8b are found in 8ab. In addition, the expression of the structural protein, envelope (E), was down-regulated by 8b but not 8a or 8ab. Consequently, E was not detectable in SARS-CoV-infected cells that were expressing high levels of 8b. These findings suggest that 8b may modulate viral replication and/or pathogenesis.</div>
</front>
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<Abstract><AbstractText>The severe acute respiratory syndrome coronavirus (SARS-CoV), isolated from humans infected during the peak of epidemic, encodes two accessory proteins termed as 8a and 8b. Interestingly, the SARS-CoV isolated from animals contains an extra 29-nucleotide in this region such that these proteins are fused to become a single protein, 8ab. Here, we compared the cellular properties of the 8a, 8b and 8ab proteins by examining their cellular localizations and their abilities to interact with other SARS-CoV proteins. These results may suggest that the conformations of 8a and 8b are different from 8ab although nearly all the amino acids in 8a and 8b are found in 8ab. In addition, the expression of the structural protein, envelope (E), was down-regulated by 8b but not 8a or 8ab. Consequently, E was not detectable in SARS-CoV-infected cells that were expressing high levels of 8b. These findings suggest that 8b may modulate viral replication and/or pathogenesis.</AbstractText>
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The human severe acute respiratory syndrome coronavirus (SARS-CoV) 8b protein is distinct from its counterpart in animal SARS-CoV and down-regulates the expression of the envelope protein in infected cells.

The human severe acute respiratory syndrome coronavirus (SARS-CoV) 8b protein is distinct from its counterpart in animal SARS-CoV and down-regulates the expression of the envelope protein in infected cells.

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