The transmembrane oligomers of coronavirus protein E.
Identifieur interne : 002885 ( PubMed/Corpus ); précédent : 002884; suivant : 002886The transmembrane oligomers of coronavirus protein E.
Auteurs : Jaume Torres ; Jifeng Wang ; Krupakar Parthasarathy ; Ding Xiang LiuSource :
- Biophysical journal [ 0006-3495 ] ; 2005.
English descriptors
- KwdEn :
- Binding Sites, Cell Membrane (chemistry), Computer Simulation, Dimerization, Lipid Bilayers (chemistry), Models, Chemical, Models, Molecular, Multiprotein Complexes (analysis), Multiprotein Complexes (chemistry), Multiprotein Complexes (ultrastructure), Protein Binding, Protein Conformation, Viral Envelope Proteins (analysis), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (ultrastructure).
- MESH :
- chemical , analysis : Multiprotein Complexes, Viral Envelope Proteins.
- chemical , chemistry : Lipid Bilayers, Multiprotein Complexes, Viral Envelope Proteins.
- chemistry : Cell Membrane.
- chemical , ultrastructure : Multiprotein Complexes, Viral Envelope Proteins.
- Binding Sites, Computer Simulation, Dimerization, Models, Chemical, Models, Molecular, Protein Binding, Protein Conformation.
Abstract
We have tested the hypothesis that severe acute respiratory syndrome (SARS) coronavirus protein E (SCoVE) and its homologs in other coronaviruses associate through their putative transmembrane domain to form homooligomeric alpha-helical bundles in vivo. For this purpose, we have analyzed the results of molecular dynamics simulations where all possible conformational and aggregational space was systematically explored. Two main assumptions were considered; the first is that protein E contains one transmembrane alpha-helical domain, with its N- and C-termini located in opposite faces of the lipid bilayer. The second is that protein E forms the same type of transmembrane oligomer and with identical backbone structure in different coronaviruses. The models arising from the molecular dynamics simulations were tested for evolutionary conservation using 13 coronavirus protein E homologous sequences. It is extremely unlikely that if any of our assumptions were not correct we would find a persistent structure for all the sequences tested. We show that a low energy dimeric, trimeric and two pentameric models appear to be conserved through evolution, and are therefore likely to be present in vivo. In support of this, we have observed only dimeric, trimeric, and pentameric aggregates for the synthetic transmembrane domain of SARS protein E in SDS. The models obtained point to residues essential for protein E oligomerization in the life cycle of the SARS virus, specifically N15. In addition, these results strongly support a general model where transmembrane domains transiently adopt many aggregation states necessary for function.
DOI: 10.1529/biophysj.104.051730
PubMed: 15713601
Links to Exploration step
pubmed:15713601Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The transmembrane oligomers of coronavirus protein E.</title><author><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name><affiliation><nlm:affiliation>School of Biological Sciences, Nanyang Technological University, Singapore. jtorres@ntu.edu.sg</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Jifeng" sort="Wang, Jifeng" uniqKey="Wang J" first="Jifeng" last="Wang">Jifeng Wang</name></author><author><name sortKey="Parthasarathy, Krupakar" sort="Parthasarathy, Krupakar" uniqKey="Parthasarathy K" first="Krupakar" last="Parthasarathy">Krupakar Parthasarathy</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></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15713601</idno><idno type="pmid">15713601</idno><idno type="doi">10.1529/biophysj.104.051730</idno><idno type="wicri:Area/PubMed/Corpus">002885</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002885</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The transmembrane oligomers of coronavirus protein E.</title><author><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name><affiliation><nlm:affiliation>School of Biological Sciences, Nanyang Technological University, Singapore. jtorres@ntu.edu.sg</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Jifeng" sort="Wang, Jifeng" uniqKey="Wang J" first="Jifeng" last="Wang">Jifeng Wang</name></author><author><name sortKey="Parthasarathy, Krupakar" sort="Parthasarathy, Krupakar" uniqKey="Parthasarathy K" first="Krupakar" last="Parthasarathy">Krupakar Parthasarathy</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="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Cell Membrane (chemistry)</term><term>Computer Simulation</term><term>Dimerization</term><term>Lipid Bilayers (chemistry)</term><term>Models, Chemical</term><term>Models, Molecular</term><term>Multiprotein Complexes (analysis)</term><term>Multiprotein Complexes (chemistry)</term><term>Multiprotein Complexes (ultrastructure)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Viral Envelope Proteins (analysis)</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (ultrastructure)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Multiprotein Complexes</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lipid Bilayers</term><term>Multiprotein Complexes</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Multiprotein Complexes</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Computer Simulation</term><term>Dimerization</term><term>Models, Chemical</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Conformation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have tested the hypothesis that severe acute respiratory syndrome (SARS) coronavirus protein E (SCoVE) and its homologs in other coronaviruses associate through their putative transmembrane domain to form homooligomeric alpha-helical bundles in vivo. For this purpose, we have analyzed the results of molecular dynamics simulations where all possible conformational and aggregational space was systematically explored. Two main assumptions were considered; the first is that protein E contains one transmembrane alpha-helical domain, with its N- and C-termini located in opposite faces of the lipid bilayer. The second is that protein E forms the same type of transmembrane oligomer and with identical backbone structure in different coronaviruses. The models arising from the molecular dynamics simulations were tested for evolutionary conservation using 13 coronavirus protein E homologous sequences. It is extremely unlikely that if any of our assumptions were not correct we would find a persistent structure for all the sequences tested. We show that a low energy dimeric, trimeric and two pentameric models appear to be conserved through evolution, and are therefore likely to be present in vivo. In support of this, we have observed only dimeric, trimeric, and pentameric aggregates for the synthetic transmembrane domain of SARS protein E in SDS. The models obtained point to residues essential for protein E oligomerization in the life cycle of the SARS virus, specifically N15. In addition, these results strongly support a general model where transmembrane domains transiently adopt many aggregation states necessary for function.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15713601</PMID><DateCompleted><Year>2005</Year><Month>07</Month><Day>05</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3495</ISSN><JournalIssue CitedMedium="Print"><Volume>88</Volume><Issue>2</Issue><PubDate><Year>2005</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Biophysical journal</Title><ISOAbbreviation>Biophys. J.</ISOAbbreviation></Journal><ArticleTitle>The transmembrane oligomers of coronavirus protein E.</ArticleTitle><Pagination><MedlinePgn>1283-90</MedlinePgn></Pagination><Abstract><AbstractText>We have tested the hypothesis that severe acute respiratory syndrome (SARS) coronavirus protein E (SCoVE) and its homologs in other coronaviruses associate through their putative transmembrane domain to form homooligomeric alpha-helical bundles in vivo. For this purpose, we have analyzed the results of molecular dynamics simulations where all possible conformational and aggregational space was systematically explored. Two main assumptions were considered; the first is that protein E contains one transmembrane alpha-helical domain, with its N- and C-termini located in opposite faces of the lipid bilayer. The second is that protein E forms the same type of transmembrane oligomer and with identical backbone structure in different coronaviruses. The models arising from the molecular dynamics simulations were tested for evolutionary conservation using 13 coronavirus protein E homologous sequences. It is extremely unlikely that if any of our assumptions were not correct we would find a persistent structure for all the sequences tested. We show that a low energy dimeric, trimeric and two pentameric models appear to be conserved through evolution, and are therefore likely to be present in vivo. In support of this, we have observed only dimeric, trimeric, and pentameric aggregates for the synthetic transmembrane domain of SARS protein E in SDS. The models obtained point to residues essential for protein E oligomerization in the life cycle of the SARS virus, specifically N15. In addition, these results strongly support a general model where transmembrane domains transiently adopt many aggregation states necessary for function.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Torres</LastName><ForeName>Jaume</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore. jtorres@ntu.edu.sg</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Jifeng</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Parthasarathy</LastName><ForeName>Krupakar</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Ding Xiang</ForeName><Initials>DX</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D023362">Evaluation Study</PublicationType><PublicationType 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