A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein.
Identifieur interne : 005494 ( Main/Exploration ); précédent : 005493; suivant : 005495A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein.
Auteurs : Eyal Arbely [Israël] ; Ziad Khattari ; Guillaume Brotons ; Mutaz Akkawi ; Tim Salditt ; Isaiah T. ArkinSource :
- Journal of molecular biology [ 0022-2836 ] ; 2004.
Descripteurs français
- KwdFr :
- Coronavirus (métabolisme), Diffusion de rayonnements, Données de séquences moléculaires, Double couche lipidique (), Membrane cellulaire (métabolisme), Microscopie électronique, Modèles moléculaires, Protéines de l'enveloppe virale (), Rayons X, Similitude de séquences d'acides aminés, Spectroscopie infrarouge à transformée de Fourier, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Thermodynamique, Virus du SRAS.
- MESH :
- métabolisme : Coronavirus, Membrane cellulaire.
- Diffusion de rayonnements, Données de séquences moléculaires, Double couche lipidique, Microscopie électronique, Modèles moléculaires, Protéines de l'enveloppe virale, Rayons X, Similitude de séquences d'acides aminés, Spectroscopie infrarouge à transformée de Fourier, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Thermodynamique, Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Sequence, Cell Membrane (metabolism), Coronavirus (metabolism), Lipid Bilayers (chemistry), Microscopy, Electron, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Protein Structure, Tertiary, SARS Virus, Scattering, Radiation, Sequence Homology, Amino Acid, Spectroscopy, Fourier Transform Infrared, Thermodynamics, Viral Envelope Proteins (chemistry), X-Rays.
- MESH :
- chemical , chemistry : Lipid Bilayers, Viral Envelope Proteins.
- metabolism : Cell Membrane, Coronavirus.
- Amino Acid Sequence, Microscopy, Electron, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Protein Structure, Tertiary, SARS Virus, Scattering, Radiation, Sequence Homology, Amino Acid, Spectroscopy, Fourier Transform Infrared, Thermodynamics, X-Rays.
Abstract
The agent responsible for the recent severe acute respiratory syndrome (SARS) outbreak is a previously unidentified coronavirus. While there is a wealth of epidemiological studies, little if any molecular characterization of SARS coronavirus (SCoV) proteins has been carried out. Here we describe the molecular characterization of SCoV E protein, a critical component of the virus responsible for virion envelope morphogenesis. We conclusively show that SCoV E protein contains an unusually short, palindromic transmembrane helical hairpin around a previously unidentified pseudo-center of symmetry, a structural feature which seems to be unique to SCoV. The hairpin deforms lipid bilayers by way of increasing their curvature, providing for the first time a molecular explanation of E protein's pivotal role in viral budding. The molecular understanding of this critical component of SCoV may represent the beginning of a concerted effort aimed at inhibiting its function, and consequently, viral infectivity.
Url:
DOI: 10.1016/j.jmb.2004.06.044
PubMed: 15288785
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 002C38
- to stream PubMed, to step Curation: 002C38
- to stream PubMed, to step Checkpoint: 002E64
- to stream Ncbi, to step Merge: 000976
- to stream Ncbi, to step Curation: 000976
- to stream Ncbi, to step Checkpoint: 000976
- to stream Hal, to step Corpus: 000002
- to stream Hal, to step Curation: 000002
- to stream Hal, to step Checkpoint: 000190
- to stream Main, to step Merge: 005939
- to stream Main, to step Curation: 005494
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein.</title><author><name sortKey="Arbely, Eyal" sort="Arbely, Eyal" uniqKey="Arbely E" first="Eyal" last="Arbely">Eyal Arbely</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University, Givat-Ram, Jerusalem 91904, Israel.</nlm:affiliation><country xml:lang="fr">Israël</country><wicri:regionArea>Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University, Givat-Ram, Jerusalem 91904</wicri:regionArea><wicri:noRegion>Jerusalem 91904</wicri:noRegion></affiliation></author><author><name sortKey="Khattari, Ziad" sort="Khattari, Ziad" uniqKey="Khattari Z" first="Ziad" last="Khattari">Ziad Khattari</name></author><author><name sortKey="Brotons, Guillaume" sort="Brotons, Guillaume" uniqKey="Brotons G" first="Guillaume" last="Brotons">Guillaume Brotons</name></author><author><name sortKey="Akkawi, Mutaz" sort="Akkawi, Mutaz" uniqKey="Akkawi M" first="Mutaz" last="Akkawi">Mutaz Akkawi</name></author><author><name sortKey="Salditt, Tim" sort="Salditt, Tim" uniqKey="Salditt T" first="Tim" last="Salditt">Tim Salditt</name></author><author><name sortKey="Arkin, Isaiah T" sort="Arkin, Isaiah T" uniqKey="Arkin I" first="Isaiah T" last="Arkin">Isaiah T. Arkin</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:15288785</idno><idno type="pmid">15288785</idno><idno type="doi">10.1016/j.jmb.2004.06.044</idno><idno type="wicri:Area/PubMed/Corpus">002C38</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002C38</idno><idno type="wicri:Area/PubMed/Curation">002C38</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002C38</idno><idno type="wicri:Area/PubMed/Checkpoint">002E64</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002E64</idno><idno type="wicri:Area/Ncbi/Merge">000976</idno><idno type="wicri:Area/Ncbi/Curation">000976</idno><idno type="wicri:Area/Ncbi/Checkpoint">000976</idno><idno type="wicri:doubleKey">0022-2836:2004:Arbely E:a:highly:unusual</idno><idno type="wicri:source">HAL</idno><idno type="RBID">Hal:hal-02538725</idno><idno type="url">https://hal-univ-lemans.archives-ouvertes.fr/hal-02538725</idno><idno type="wicri:Area/Hal/Corpus">000002</idno><idno type="wicri:Area/Hal/Curation">000002</idno><idno type="wicri:Area/Hal/Checkpoint">000190</idno><idno type="wicri:explorRef" wicri:stream="Hal" wicri:step="Checkpoint">000190</idno><idno type="wicri:doubleKey">0022-2836:2004:Arbely E:a:highly:unusual</idno><idno type="wicri:Area/Main/Merge">005939</idno><idno type="wicri:Area/Main/Curation">005494</idno><idno type="wicri:Area/Main/Exploration">005494</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein.</title><author><name sortKey="Arbely, Eyal" sort="Arbely, Eyal" uniqKey="Arbely E" first="Eyal" last="Arbely">Eyal Arbely</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University, Givat-Ram, Jerusalem 91904, Israel.</nlm:affiliation><country xml:lang="fr">Israël</country><wicri:regionArea>Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University, Givat-Ram, Jerusalem 91904</wicri:regionArea><wicri:noRegion>Jerusalem 91904</wicri:noRegion></affiliation></author><author><name sortKey="Khattari, Ziad" sort="Khattari, Ziad" uniqKey="Khattari Z" first="Ziad" last="Khattari">Ziad Khattari</name></author><author><name sortKey="Brotons, Guillaume" sort="Brotons, Guillaume" uniqKey="Brotons G" first="Guillaume" last="Brotons">Guillaume Brotons</name></author><author><name sortKey="Akkawi, Mutaz" sort="Akkawi, Mutaz" uniqKey="Akkawi M" first="Mutaz" last="Akkawi">Mutaz Akkawi</name></author><author><name sortKey="Salditt, Tim" sort="Salditt, Tim" uniqKey="Salditt T" first="Tim" last="Salditt">Tim Salditt</name></author><author><name sortKey="Arkin, Isaiah T" sort="Arkin, Isaiah T" uniqKey="Arkin I" first="Isaiah T" last="Arkin">Isaiah T. Arkin</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="ISSN">0022-2836</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Cell Membrane (metabolism)</term><term>Coronavirus (metabolism)</term><term>Lipid Bilayers (chemistry)</term><term>Microscopy, Electron</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>SARS Virus</term><term>Scattering, Radiation</term><term>Sequence Homology, Amino Acid</term><term>Spectroscopy, Fourier Transform Infrared</term><term>Thermodynamics</term><term>Viral Envelope Proteins (chemistry)</term><term>X-Rays</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Coronavirus (métabolisme)</term><term>Diffusion de rayonnements</term><term>Données de séquences moléculaires</term><term>Double couche lipidique ()</term><term>Membrane cellulaire (métabolisme)</term><term>Microscopie électronique</term><term>Modèles moléculaires</term><term>Protéines de l'enveloppe virale ()</term><term>Rayons X</term><term>Similitude de séquences d'acides aminés</term><term>Spectroscopie infrarouge à transformée de Fourier</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Thermodynamique</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lipid Bilayers</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Coronavirus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Coronavirus</term><term>Membrane cellulaire</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Microscopy, Electron</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>SARS Virus</term><term>Scattering, Radiation</term><term>Sequence Homology, Amino Acid</term><term>Spectroscopy, Fourier Transform Infrared</term><term>Thermodynamics</term><term>X-Rays</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Diffusion de rayonnements</term><term>Données de séquences moléculaires</term><term>Double couche lipidique</term><term>Microscopie électronique</term><term>Modèles moléculaires</term><term>Protéines de l'enveloppe virale</term><term>Rayons X</term><term>Similitude de séquences d'acides aminés</term><term>Spectroscopie infrarouge à transformée de Fourier</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Thermodynamique</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The agent responsible for the recent severe acute respiratory syndrome (SARS) outbreak is a previously unidentified coronavirus. While there is a wealth of epidemiological studies, little if any molecular characterization of SARS coronavirus (SCoV) proteins has been carried out. Here we describe the molecular characterization of SCoV E protein, a critical component of the virus responsible for virion envelope morphogenesis. We conclusively show that SCoV E protein contains an unusually short, palindromic transmembrane helical hairpin around a previously unidentified pseudo-center of symmetry, a structural feature which seems to be unique to SCoV. The hairpin deforms lipid bilayers by way of increasing their curvature, providing for the first time a molecular explanation of E protein's pivotal role in viral budding. The molecular understanding of this critical component of SCoV may represent the beginning of a concerted effort aimed at inhibiting its function, and consequently, viral infectivity.</div></front></TEI><affiliations><list><country><li>Israël</li></country></list><tree><noCountry><name sortKey="Akkawi, Mutaz" sort="Akkawi, Mutaz" uniqKey="Akkawi M" first="Mutaz" last="Akkawi">Mutaz Akkawi</name><name sortKey="Arkin, Isaiah T" sort="Arkin, Isaiah T" uniqKey="Arkin I" first="Isaiah T" last="Arkin">Isaiah T. Arkin</name><name sortKey="Brotons, Guillaume" sort="Brotons, Guillaume" uniqKey="Brotons G" first="Guillaume" last="Brotons">Guillaume Brotons</name><name sortKey="Khattari, Ziad" sort="Khattari, Ziad" uniqKey="Khattari Z" first="Ziad" last="Khattari">Ziad Khattari</name><name sortKey="Salditt, Tim" sort="Salditt, Tim" uniqKey="Salditt T" first="Tim" last="Salditt">Tim Salditt</name></noCountry><country name="Israël"><noRegion><name sortKey="Arbely, Eyal" sort="Arbely, Eyal" uniqKey="Arbely E" first="Eyal" last="Arbely">Eyal Arbely</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 005494 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 005494 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:15288785
|texte= A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:15288785" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |