Enhancement of murine coronavirus replication by severe acute respiratory syndrome coronavirus protein 6 requires the N-terminal hydrophobic region but not C-terminal sorting motifs.
Identifieur interne : 003717 ( Main/Curation ); précédent : 003716; suivant : 003718Enhancement of murine coronavirus replication by severe acute respiratory syndrome coronavirus protein 6 requires the N-terminal hydrophobic region but not C-terminal sorting motifs.
Auteurs : Jason Netland [États-Unis] ; Debra Ferraro ; Lecia Pewe ; Heidi Olivares ; Thomas Gallagher ; Stanley PerlmanSource :
- Journal of virology [ 0022-538X ] ; 2007.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Protéines virales.
- physiologie : Protéines virales.
- Animaux, Infections à coronavirus, Interactions hydrophobes et hydrophiles, Motifs d'acides aminés, Mutation, Protéines virales, Réplication virale, Souris, Virus du SRAS.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Viral Proteins.
- chemistry : SARS Virus.
- chemical , genetics : Viral Proteins.
- chemical , physiology : Viral Proteins.
- Amino Acid Motifs, Animals, Coronavirus Infections, Hydrophobic and Hydrophilic Interactions, Mice, Mutation, Virus Replication.
Abstract
Severe acute respiratory syndrome coronavirus encodes several accessory proteins of unknown function. We previously showed that one such protein, encoded by ORF6, enhanced the growth of mouse hepatitis virus in tissue culture cells and in mice. Protein 6 consists of an N-terminal hydrophobic peptide and a C-terminal region containing intracellular protein sorting motifs. Herein, we show that mutation of the hydrophobic region but not the sorting motifs affected the ability of protein 6 to enhance virus growth. Collectively, these results support the notion that the 6 protein interacts with membrane-bound viral replication or assembly machinery to directly enhance virus replication and virulence in animals.
DOI: 10.1128/JVI.01308-07
PubMed: 17670827
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pubmed:17670827Le document en format XML
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<term>Mice</term>
<term>Mutation</term>
<term>SARS Virus (chemistry)</term>
<term>Viral Proteins (chemistry)</term>
<term>Viral Proteins (genetics)</term>
<term>Viral Proteins (physiology)</term>
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<term>Interactions hydrophobes et hydrophiles</term>
<term>Motifs d'acides aminés</term>
<term>Mutation</term>
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<term>Réplication virale</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus encodes several accessory proteins of unknown function. We previously showed that one such protein, encoded by ORF6, enhanced the growth of mouse hepatitis virus in tissue culture cells and in mice. Protein 6 consists of an N-terminal hydrophobic peptide and a C-terminal region containing intracellular protein sorting motifs. Herein, we show that mutation of the hydrophobic region but not the sorting motifs affected the ability of protein 6 to enhance virus growth. Collectively, these results support the notion that the 6 protein interacts with membrane-bound viral replication or assembly machinery to directly enhance virus replication and virulence in animals.</div>
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