Structural model of the SARS coronavirus E channel in LMPG micelles
Identifieur interne : 000796 ( Main/Exploration ); précédent : 000795; suivant : 000797Structural model of the SARS coronavirus E channel in LMPG micelles
Auteurs : Wahyu Surya ; Yan Li ; Jaume TorresSource :
- Biochimica et Biophysica Acta. Biomembranes [ 0005-2736 ] ; 2018.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Phosphatidylglycerols, Viral Envelope Proteins.
- chemical : Micelles.
- chemistry : SARS Virus.
- Electrophoresis, Polyacrylamide Gel, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Structure-Activity Relationship.
Abstract
Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly α-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation.
Url:
DOI: 10.1016/j.bbamem.2018.02.017
PubMed: 29474890
PubMed Central: 7094280
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structural model of the SARS coronavirus E channel in LMPG micelles</title><author><name sortKey="Surya, Wahyu" sort="Surya, Wahyu" uniqKey="Surya W" first="Wahyu" last="Surya">Wahyu Surya</name></author><author><name sortKey="Li, Yan" sort="Li, Yan" uniqKey="Li Y" first="Yan" last="Li">Yan Li</name></author><author><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">29474890</idno><idno type="pmc">7094280</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094280</idno><idno type="RBID">PMC:7094280</idno><idno type="doi">10.1016/j.bbamem.2018.02.017</idno><date when="2018">2018</date><idno type="wicri:Area/Pmc/Corpus">000B06</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000B06</idno><idno type="wicri:Area/Pmc/Curation">000B06</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000B06</idno><idno type="wicri:Area/Pmc/Checkpoint">000460</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000460</idno><idno type="wicri:source">PubMed</idno><idno type="RBID">pubmed:29474890</idno><idno type="wicri:Area/PubMed/Corpus">000994</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000994</idno><idno type="wicri:Area/PubMed/Curation">000994</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000994</idno><idno type="wicri:Area/PubMed/Checkpoint">000756</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000756</idno><idno type="wicri:Area/Ncbi/Merge">001D38</idno><idno type="wicri:Area/Ncbi/Curation">001D38</idno><idno type="wicri:Area/Ncbi/Checkpoint">001D38</idno><idno type="wicri:doubleKey">0005-2736:2018:Surya W:structural:model:of</idno><idno type="wicri:Area/Main/Merge">000799</idno><idno type="wicri:Area/Main/Curation">000796</idno><idno type="wicri:Area/Main/Exploration">000796</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structural model of the SARS coronavirus E channel in LMPG micelles</title><author><name sortKey="Surya, Wahyu" sort="Surya, Wahyu" uniqKey="Surya W" first="Wahyu" last="Surya">Wahyu Surya</name></author><author><name sortKey="Li, Yan" sort="Li, Yan" uniqKey="Li Y" first="Yan" last="Li">Yan Li</name></author><author><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name></author></analytic><series><title level="j">Biochimica et Biophysica Acta. Biomembranes</title><idno type="ISSN">0005-2736</idno><idno type="eISSN">1879-2642</idno><imprint><date when="2018">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Electrophoresis, Polyacrylamide Gel</term><term>Micelles</term><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Phosphatidylglycerols (chemistry)</term><term>Protein Conformation</term><term>SARS Virus (chemistry)</term><term>Structure-Activity Relationship</term><term>Viral Envelope Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines</term><term>Micelles</term><term>Modèles moléculaires</term><term>Phosphatidylglycérol ()</term><term>Protéines de l'enveloppe virale ()</term><term>Relation structure-activité</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Virus du SRAS ()</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Phosphatidylglycerols</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Micelles</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electrophoresis, Polyacrylamide Gel</term><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Conformation</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Micelles</term><term>Modèles moléculaires</term><term>Phosphatidylglycérol</term><term>Protéines de l'enveloppe virale</term><term>Relation structure-activité</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Virus du SRAS</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly α-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Holmes, K V" uniqKey="Holmes K">K.V. 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Friesen</name></author><author><name sortKey="Poolman, B" uniqKey="Poolman B">B. Poolman</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Li, Yan" sort="Li, Yan" uniqKey="Li Y" first="Yan" last="Li">Yan Li</name><name sortKey="Surya, Wahyu" sort="Surya, Wahyu" uniqKey="Surya W" first="Wahyu" last="Surya">Wahyu Surya</name><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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