A Coronavirus E Protein Is Present in Two Distinct Pools with Different Effects on Assembly and the Secretory Pathway.
Identifieur interne : 001383 ( Main/Exploration ); précédent : 001382; suivant : 001384A Coronavirus E Protein Is Present in Two Distinct Pools with Different Effects on Assembly and the Secretory Pathway.
Auteurs : Jason W. Westerbeck [États-Unis] ; Carolyn E. Machamer [États-Unis]Source :
- Journal of virology [ 1098-5514 ] ; 2015.
Descripteurs français
- KwdFr :
- Animaux, Assemblage viral (physiologie), Cellules HeLa, Cellules Vero, Humains, Multimérisation de protéines (physiologie), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Souris, Structure quaternaire des protéines, Syndrome respiratoire aigu sévère (génétique), Syndrome respiratoire aigu sévère (métabolisme), Virus du SRAS (physiologie).
- MESH :
- génétique : Protéines de l'enveloppe virale, Syndrome respiratoire aigu sévère.
- métabolisme : Protéines de l'enveloppe virale, Syndrome respiratoire aigu sévère.
- physiologie : Assemblage viral, Multimérisation de protéines, Virus du SRAS.
- Animaux, Cellules HeLa, Cellules Vero, Humains, Protéines de l'enveloppe virale, Souris, Structure quaternaire des protéines.
English descriptors
- KwdEn :
- Animals, Chlorocebus aethiops, HeLa Cells, Humans, Mice, Protein Multimerization (physiology), Protein Structure, Quaternary, SARS Virus (physiology), Severe Acute Respiratory Syndrome (genetics), Severe Acute Respiratory Syndrome (metabolism), Vero Cells, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virus Assembly (physiology).
- MESH :
- chemical , chemistry : Viral Envelope Proteins.
- genetics : Severe Acute Respiratory Syndrome, Viral Envelope Proteins.
- metabolism : Severe Acute Respiratory Syndrome, Viral Envelope Proteins.
- physiology : Protein Multimerization, SARS Virus, Virus Assembly.
- Animals, Chlorocebus aethiops, HeLa Cells, Humans, Mice, Protein Structure, Quaternary, Vero Cells.
Abstract
Coronaviruses (CoVs) assemble by budding into the lumen of the early Golgi complex prior to exocytosis. The small CoV envelope (E) protein plays roles in assembly, virion release, and pathogenesis. CoV E has a single hydrophobic domain (HD), is targeted to Golgi complex membranes, and has cation channel activity in vitro. However, the precise functions of the CoV E protein during infection are still enigmatic. Structural data for the severe acute respiratory syndrome (SARS)-CoV E protein suggest that it assembles into a homopentamer. Specific residues in the HD regulate the ion-conducting pore formed by SARS-CoV E in artificial bilayers and the pathogenicity of the virus during infection. The E protein from the avian infectious bronchitis virus (IBV) has dramatic effects on the secretory system which require residues in the HD. Here, we use the known structural data from SARS-CoV E to infer the residues important for ion channel activity and the oligomerization of IBV E. We present biochemical data for the formation of two distinct oligomeric pools of IBV E in transfected and infected cells and the residues required for their formation. A high-order oligomer of IBV E is required for the production of virus-like particles (VLPs), implicating this form of the protein in virion assembly. Additionally, disruption of the secretory pathway by IBV E correlates with a form that is likely monomeric, suggesting that the effects on the secretory pathway are independent of E ion channel activity.
DOI: 10.1128/JVI.01237-15
PubMed: 26136577
Affiliations:
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Machamer</name><affiliation wicri:level="2"><nlm:affiliation>Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA machamer@jhmi.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26136577</idno><idno type="pmid">26136577</idno><idno type="doi">10.1128/JVI.01237-15</idno><idno type="wicri:Area/PubMed/Corpus">000E05</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000E05</idno><idno type="wicri:Area/PubMed/Curation">000E05</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000E05</idno><idno type="wicri:Area/PubMed/Checkpoint">000E74</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000E74</idno><idno type="wicri:Area/Ncbi/Merge">002A92</idno><idno type="wicri:Area/Ncbi/Curation">002A92</idno><idno type="wicri:Area/Ncbi/Checkpoint">002A92</idno><idno type="wicri:Area/Main/Merge">001385</idno><idno type="wicri:Area/Main/Curation">001383</idno><idno type="wicri:Area/Main/Exploration">001383</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A Coronavirus E Protein Is Present in Two Distinct Pools with Different Effects on Assembly and the Secretory Pathway.</title><author><name sortKey="Westerbeck, Jason W" sort="Westerbeck, Jason W" uniqKey="Westerbeck J" first="Jason W" last="Westerbeck">Jason W. Westerbeck</name><affiliation wicri:level="2"><nlm:affiliation>Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Machamer, Carolyn E" sort="Machamer, Carolyn E" uniqKey="Machamer C" first="Carolyn E" last="Machamer">Carolyn E. Machamer</name><affiliation wicri:level="2"><nlm:affiliation>Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA machamer@jhmi.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>HeLa Cells</term><term>Humans</term><term>Mice</term><term>Protein Multimerization (physiology)</term><term>Protein Structure, Quaternary</term><term>SARS Virus (physiology)</term><term>Severe Acute Respiratory Syndrome (genetics)</term><term>Severe Acute Respiratory Syndrome (metabolism)</term><term>Vero Cells</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term><term>Virus Assembly (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Assemblage viral (physiologie)</term><term>Cellules HeLa</term><term>Cellules Vero</term><term>Humains</term><term>Multimérisation de protéines (physiologie)</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Souris</term><term>Structure quaternaire des protéines</term><term>Syndrome respiratoire aigu sévère (génétique)</term><term>Syndrome respiratoire aigu sévère (métabolisme)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de l'enveloppe virale</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines de l'enveloppe virale</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Assemblage viral</term><term>Multimérisation de protéines</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protein Multimerization</term><term>SARS Virus</term><term>Virus Assembly</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>HeLa Cells</term><term>Humans</term><term>Mice</term><term>Protein Structure, Quaternary</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HeLa</term><term>Cellules Vero</term><term>Humains</term><term>Protéines de l'enveloppe virale</term><term>Souris</term><term>Structure quaternaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronaviruses (CoVs) assemble by budding into the lumen of the early Golgi complex prior to exocytosis. The small CoV envelope (E) protein plays roles in assembly, virion release, and pathogenesis. CoV E has a single hydrophobic domain (HD), is targeted to Golgi complex membranes, and has cation channel activity in vitro. However, the precise functions of the CoV E protein during infection are still enigmatic. Structural data for the severe acute respiratory syndrome (SARS)-CoV E protein suggest that it assembles into a homopentamer. Specific residues in the HD regulate the ion-conducting pore formed by SARS-CoV E in artificial bilayers and the pathogenicity of the virus during infection. The E protein from the avian infectious bronchitis virus (IBV) has dramatic effects on the secretory system which require residues in the HD. Here, we use the known structural data from SARS-CoV E to infer the residues important for ion channel activity and the oligomerization of IBV E. We present biochemical data for the formation of two distinct oligomeric pools of IBV E in transfected and infected cells and the residues required for their formation. A high-order oligomer of IBV E is required for the production of virus-like particles (VLPs), implicating this form of the protein in virion assembly. Additionally, disruption of the secretory pathway by IBV E correlates with a form that is likely monomeric, suggesting that the effects on the secretory pathway are independent of E ion channel activity.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><country name="États-Unis"><region name="Maryland"><name sortKey="Westerbeck, Jason W" sort="Westerbeck, Jason W" uniqKey="Westerbeck J" first="Jason W" last="Westerbeck">Jason W. Westerbeck</name></region><name sortKey="Machamer, Carolyn E" sort="Machamer, Carolyn E" uniqKey="Machamer C" first="Carolyn E" last="Machamer">Carolyn E. 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