Model of a putative pore: the pentameric alpha-helical bundle of SARS coronavirus E protein in lipid bilayers.
Identifieur interne : 003E20 ( Main/Exploration ); précédent : 003E19; suivant : 003E21Model of a putative pore: the pentameric alpha-helical bundle of SARS coronavirus E protein in lipid bilayers.
Auteurs : Jaume Torres [Singapour] ; Krupakar Parthasarathy ; Xin Lin ; Rathi Saravanan ; Andreas Kukol ; Ding Xiang LiuSource :
- Biophysical journal [ 0006-3495 ] ; 2006.
Descripteurs français
- KwdFr :
- Conformation des protéines, Dimérisation, Données de séquences moléculaires, Double couche lipidique (), Escherichia coli (métabolisme), Membrane cellulaire (métabolisme), Modèles moléculaires, Phénylalanine (pharmacologie), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (métabolisme), Similitude de séquences d'acides aminés, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Virus du SRAS (métabolisme).
- MESH :
- métabolisme : Escherichia coli, Membrane cellulaire, Protéines de l'enveloppe virale, Virus du SRAS.
- pharmacologie : Phénylalanine.
- Conformation des protéines, Dimérisation, Données de séquences moléculaires, Double couche lipidique, Modèles moléculaires, Protéines de l'enveloppe virale, Similitude de séquences d'acides aminés, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Cell Membrane (metabolism), Dimerization, Escherichia coli (metabolism), Lipid Bilayers (chemistry), Models, Molecular, Molecular Sequence Data, Phenylalanine (pharmacology), Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, SARS Virus (metabolism), Sequence Homology, Amino Acid, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Lipid Bilayers, Viral Envelope Proteins.
- metabolism : Cell Membrane, Escherichia coli, SARS Virus, Viral Envelope Proteins.
- chemical , pharmacology : Phenylalanine.
- Amino Acid Sequence, Dimerization, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid.
Abstract
The coronavirus responsible for the severe acute respiratory syndrome contains a small envelope protein, E, with putative involvement in host apoptosis and virus morphogenesis. To perform these functions, it has been suggested that protein E can form a membrane destabilizing transmembrane (TM) hairpin, or homooligomerize to form a TM pore. Indeed, in a recent study we reported that the alpha-helical putative transmembrane domain of E protein (ETM) forms several SDS-resistant TM interactions: a dimer, a trimer, and two pentameric forms. Further, these interactions were found to be evolutionarily conserved. Herein, we have studied multiple isotopically labeled ETM peptides reconstituted in model lipid bilayers, using the orientational parameters derived from infrared dichroic data. We show that the topology of ETM is consistent with a regular TM alpha-helix. Further, the orientational parameters obtained unequivocally correspond to a homopentameric model, by comparison with previous predictions. We have independently confirmed that the full polypeptide of E protein can also aggregate as pentamers after expression in Escherichia coli. This interaction must be stabilized, at least partially, at the TM domain. The model we report for this pentameric alpha-helical bundle may explain some of the permabilizing properties of protein E, and should be the basis of mutagenesis efforts in future functional studies.
DOI: 10.1529/biophysj.105.080119
PubMed: 16698774
Affiliations:
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Le document en format XML
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xml:lang="fr">Singapour</country><wicri:regionArea>School of Biological Sciences, Nanyang Technological University</wicri:regionArea><wicri:noRegion>Nanyang Technological University</wicri:noRegion></affiliation></author><author><name sortKey="Parthasarathy, Krupakar" sort="Parthasarathy, Krupakar" uniqKey="Parthasarathy K" first="Krupakar" last="Parthasarathy">Krupakar Parthasarathy</name></author><author><name sortKey="Lin, Xin" sort="Lin, Xin" uniqKey="Lin X" first="Xin" last="Lin">Xin Lin</name></author><author><name sortKey="Saravanan, Rathi" sort="Saravanan, Rathi" uniqKey="Saravanan R" first="Rathi" last="Saravanan">Rathi Saravanan</name></author><author><name sortKey="Kukol, Andreas" sort="Kukol, Andreas" uniqKey="Kukol A" first="Andreas" last="Kukol">Andreas Kukol</name></author><author><name sortKey="Liu, Ding Xiang" sort="Liu, Ding Xiang" uniqKey="Liu D" first="Ding Xiang" last="Liu">Ding Xiang Liu</name></author></analytic><series><title level="j">Biophysical journal</title><idno type="ISSN">0006-3495</idno><imprint><date when="2006" type="published">2006</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>Dimerization</term><term>Escherichia coli (metabolism)</term><term>Lipid Bilayers (chemistry)</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Phenylalanine (pharmacology)</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>SARS Virus (metabolism)</term><term>Sequence Homology, Amino Acid</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Double couche lipidique ()</term><term>Escherichia coli (métabolisme)</term><term>Membrane cellulaire (métabolisme)</term><term>Modèles moléculaires</term><term>Phénylalanine (pharmacologie)</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Similitude de séquences d'acides aminés</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus du SRAS (métabolisme)</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>Escherichia coli</term><term>SARS Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term><term>Membrane cellulaire</term><term>Protéines de l'enveloppe 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protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The coronavirus responsible for the severe acute respiratory syndrome contains a small envelope protein, E, with putative involvement in host apoptosis and virus morphogenesis. To perform these functions, it has been suggested that protein E can form a membrane destabilizing transmembrane (TM) hairpin, or homooligomerize to form a TM pore. Indeed, in a recent study we reported that the alpha-helical putative transmembrane domain of E protein (ETM) forms several SDS-resistant TM interactions: a dimer, a trimer, and two pentameric forms. Further, these interactions were found to be evolutionarily conserved. Herein, we have studied multiple isotopically labeled ETM peptides reconstituted in model lipid bilayers, using the orientational parameters derived from infrared dichroic data. We show that the topology of ETM is consistent with a regular TM alpha-helix. Further, the orientational parameters obtained unequivocally correspond to a homopentameric model, by comparison with previous predictions. We have independently confirmed that the full polypeptide of E protein can also aggregate as pentamers after expression in Escherichia coli. This interaction must be stabilized, at least partially, at the TM domain. The model we report for this pentameric alpha-helical bundle may explain some of the permabilizing properties of protein E, and should be the basis of mutagenesis efforts in future functional studies.</div></front></TEI><affiliations><list><country><li>Singapour</li></country></list><tree><noCountry><name sortKey="Kukol, Andreas" sort="Kukol, Andreas" uniqKey="Kukol A" first="Andreas" last="Kukol">Andreas Kukol</name><name sortKey="Lin, Xin" sort="Lin, Xin" uniqKey="Lin X" first="Xin" last="Lin">Xin Lin</name><name sortKey="Liu, Ding Xiang" sort="Liu, Ding Xiang" uniqKey="Liu D" first="Ding Xiang" last="Liu">Ding Xiang Liu</name><name sortKey="Parthasarathy, Krupakar" sort="Parthasarathy, Krupakar" uniqKey="Parthasarathy K" first="Krupakar" last="Parthasarathy">Krupakar Parthasarathy</name><name sortKey="Saravanan, Rathi" sort="Saravanan, Rathi" uniqKey="Saravanan R" first="Rathi" last="Saravanan">Rathi Saravanan</name></noCountry><country name="Singapour"><noRegion><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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