SrasV1, PubMed, Corpus, bibRecord, 001D55

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 : 001D55 ( PubMed/Corpus ); précédent : 001D54; suivant : 001D56

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.

Auteurs : Jason Netland ; Debra Ferraro ; Lecia Pewe ; Heidi Olivares ; Thomas Gallagher ; Stanley Perlman

Source :

Journal of virology [ 0022-538X ] ; 2007.

RBID : pubmed:17670827

English descriptors

KwdEn :
- Amino Acid Motifs, Animals, Coronavirus Infections, Hydrophobic and Hydrophilic Interactions, Mice, Mutation, SARS Virus (chemistry), Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (physiology), Virus Replication.
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

Links to Exploration step

pubmed:17670827

Le document en format XML

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<author><name sortKey="Netland, Jason" sort="Netland, Jason" uniqKey="Netland J" first="Jason" last="Netland">Jason Netland</name>
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<author><name sortKey="Ferraro, Debra" sort="Ferraro, Debra" uniqKey="Ferraro D" first="Debra" last="Ferraro">Debra Ferraro</name>
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<author><name sortKey="Pewe, Lecia" sort="Pewe, Lecia" uniqKey="Pewe L" first="Lecia" last="Pewe">Lecia Pewe</name>
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<author><name sortKey="Olivares, Heidi" sort="Olivares, Heidi" uniqKey="Olivares H" first="Heidi" last="Olivares">Heidi Olivares</name>
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<author><name sortKey="Gallagher, Thomas" sort="Gallagher, Thomas" uniqKey="Gallagher T" first="Thomas" last="Gallagher">Thomas Gallagher</name>
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<author><name sortKey="Perlman, Stanley" sort="Perlman, Stanley" uniqKey="Perlman S" first="Stanley" last="Perlman">Stanley Perlman</name>
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<term>Mice</term>
<term>Mutation</term>
<term>SARS Virus (chemistry)</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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<Abstract><AbstractText>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.</AbstractText>
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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.

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.

Source :

English descriptors

Abstract

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