Structural insights of a self-assembling 9-residue peptide from the C-terminal tail of the SARS corona virus E-protein in DPC and SDS micelles: A combined high and low resolution spectroscopic study.
Identifieur interne : 000606 ( PubMed/Corpus ); précédent : 000605; suivant : 000607Structural insights of a self-assembling 9-residue peptide from the C-terminal tail of the SARS corona virus E-protein in DPC and SDS micelles: A combined high and low resolution spectroscopic study.
Auteurs : Anirban Ghosh ; Dipita Bhattacharyya ; Anirban BhuniaSource :
- Biochimica et biophysica acta. Biomembranes [ 0005-2736 ] ; 2018.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Circular Dichroism, Humans, Lipid Bilayers (chemistry), Lipid Bilayers (metabolism), Magnetic Resonance Spectroscopy, Micelles, Models, Molecular, Oligopeptides (chemistry), Oligopeptides (metabolism), Phosphorylcholine (analogs & derivatives), Phosphorylcholine (chemistry), Protein Binding, Protein Structure, Secondary, Sodium Dodecyl Sulfate (chemistry), Unilamellar Liposomes (chemistry), Unilamellar Liposomes (metabolism), Viral Envelope Proteins (chemistry).
- MESH :
- chemical , analogs & derivatives : Phosphorylcholine.
- chemical , chemistry : Lipid Bilayers, Oligopeptides, Phosphorylcholine, Sodium Dodecyl Sulfate, Unilamellar Liposomes, Viral Envelope Proteins.
- chemical , metabolism : Lipid Bilayers, Oligopeptides, Unilamellar Liposomes.
- Amino Acid Sequence, Animals, Circular Dichroism, Humans, Magnetic Resonance Spectroscopy, Micelles, Models, Molecular, Protein Binding, Protein Structure, Secondary.
Abstract
In recent years, several studies based on the interaction of self-assembling short peptides derived from viroporins with model membranes, have improved our understanding of the molecular mechanism of corona virus (CoV) infection under physiological conditions. In this study, we have characterized the mechanism of membrane interaction of a short, 9-residue peptide TK9 (T55VYVYSRVK63) that had been derived from the carboxyl terminal of the Severe Acute Respiratory Syndrome (SARS) corona virus (SARS CoV) envelope (E) protein. The peptide has been studied for its physical changes in the presence of both zwitterionic DPC and negatively charged SDS model membrane micelles, respectively, with the help of a battery of biophysical techniques including two-dimensional solution state NMR spectroscopy. Interestingly, in both micellar environments, TK9 adopted an alpha helical conformation; however, the helical propensities were much higher in the case of DPC compared to those of SDS micelle, suggesting that TK9 has more specificity towards eukaryotic cell membrane than the bacterial cell membrane. The orientation of the peptide TK9 also varies in the different micellar environments. The peptide's affinity was further manifested by its pronounced membrane disruption ability towards the mammalian compared to the bacterial membrane mimic. Collectively, the in-depth structural information on the interaction of TK9 with different membrane environments explains the host specificity and membrane orientation owing to subsequent membrane disruption implicated in the viral pathogenesis.
DOI: 10.1016/j.bbamem.2017.10.015
PubMed: 29038024
Links to Exploration step
pubmed:29038024Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structural insights of a self-assembling 9-residue peptide from the C-terminal tail of the SARS corona virus E-protein in DPC and SDS micelles: A combined high and low resolution spectroscopic study.</title><author><name sortKey="Ghosh, Anirban" sort="Ghosh, Anirban" uniqKey="Ghosh A" first="Anirban" last="Ghosh">Anirban Ghosh</name><affiliation><nlm:affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.</nlm:affiliation></affiliation></author><author><name sortKey="Bhattacharyya, Dipita" sort="Bhattacharyya, Dipita" uniqKey="Bhattacharyya D" first="Dipita" last="Bhattacharyya">Dipita Bhattacharyya</name><affiliation><nlm:affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.</nlm:affiliation></affiliation></author><author><name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</name><affiliation><nlm:affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India. Electronic address: bhunia@jcbose.ac.in.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2018">2018</date><idno type="RBID">pubmed:29038024</idno><idno type="pmid">29038024</idno><idno type="doi">10.1016/j.bbamem.2017.10.015</idno><idno type="wicri:Area/PubMed/Corpus">000606</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000606</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structural insights of a self-assembling 9-residue peptide from the C-terminal tail of the SARS corona virus E-protein in DPC and SDS micelles: A combined high and low resolution spectroscopic study.</title><author><name sortKey="Ghosh, Anirban" sort="Ghosh, Anirban" uniqKey="Ghosh A" first="Anirban" last="Ghosh">Anirban Ghosh</name><affiliation><nlm:affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.</nlm:affiliation></affiliation></author><author><name sortKey="Bhattacharyya, Dipita" sort="Bhattacharyya, Dipita" uniqKey="Bhattacharyya D" first="Dipita" last="Bhattacharyya">Dipita Bhattacharyya</name><affiliation><nlm:affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.</nlm:affiliation></affiliation></author><author><name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</name><affiliation><nlm:affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India. Electronic address: bhunia@jcbose.ac.in.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta. Biomembranes</title><idno type="ISSN">0005-2736</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Circular Dichroism</term><term>Humans</term><term>Lipid Bilayers (chemistry)</term><term>Lipid Bilayers (metabolism)</term><term>Magnetic Resonance Spectroscopy</term><term>Micelles</term><term>Models, Molecular</term><term>Oligopeptides (chemistry)</term><term>Oligopeptides (metabolism)</term><term>Phosphorylcholine (analogs & derivatives)</term><term>Phosphorylcholine (chemistry)</term><term>Protein Binding</term><term>Protein Structure, Secondary</term><term>Sodium Dodecyl Sulfate (chemistry)</term><term>Unilamellar Liposomes (chemistry)</term><term>Unilamellar Liposomes (metabolism)</term><term>Viral Envelope Proteins (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Phosphorylcholine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lipid Bilayers</term><term>Oligopeptides</term><term>Phosphorylcholine</term><term>Sodium Dodecyl Sulfate</term><term>Unilamellar Liposomes</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lipid Bilayers</term><term>Oligopeptides</term><term>Unilamellar Liposomes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Circular Dichroism</term><term>Humans</term><term>Magnetic Resonance Spectroscopy</term><term>Micelles</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Structure, Secondary</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In recent years, several studies based on the interaction of self-assembling short peptides derived from viroporins with model membranes, have improved our understanding of the molecular mechanism of corona virus (CoV) infection under physiological conditions. In this study, we have characterized the mechanism of membrane interaction of a short, 9-residue peptide TK9 (T<sup>55</sup>VYVYSRVK<sup>63</sup>) that had been derived from the carboxyl terminal of the Severe Acute Respiratory Syndrome (SARS) corona virus (SARS CoV) envelope (E) protein. The peptide has been studied for its physical changes in the presence of both zwitterionic DPC and negatively charged SDS model membrane micelles, respectively, with the help of a battery of biophysical techniques including two-dimensional solution state NMR spectroscopy. Interestingly, in both micellar environments, TK9 adopted an alpha helical conformation; however, the helical propensities were much higher in the case of DPC compared to those of SDS micelle, suggesting that TK9 has more specificity towards eukaryotic cell membrane than the bacterial cell membrane. The orientation of the peptide TK9 also varies in the different micellar environments. The peptide's affinity was further manifested by its pronounced membrane disruption ability towards the mammalian compared to the bacterial membrane mimic. Collectively, the in-depth structural information on the interaction of TK9 with different membrane environments explains the host specificity and membrane orientation owing to subsequent membrane disruption implicated in the viral pathogenesis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29038024</PMID><DateCompleted><Year>2018</Year><Month>05</Month><Day>22</Day></DateCompleted><DateRevised><Year>2018</Year><Month>09</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0005-2736</ISSN><JournalIssue CitedMedium="Print"><Volume>1860</Volume><Issue>2</Issue><PubDate><Year>2018</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta. Biomembranes</Title><ISOAbbreviation>Biochim Biophys Acta Biomembr</ISOAbbreviation></Journal><ArticleTitle>Structural insights of a self-assembling 9-residue peptide from the C-terminal tail of the SARS corona virus E-protein in DPC and SDS micelles: A combined high and low resolution spectroscopic study.</ArticleTitle><Pagination><MedlinePgn>335-346</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0005-2736(17)30333-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbamem.2017.10.015</ELocationID><Abstract><AbstractText>In recent years, several studies based on the interaction of self-assembling short peptides derived from viroporins with model membranes, have improved our understanding of the molecular mechanism of corona virus (CoV) infection under physiological conditions. In this study, we have characterized the mechanism of membrane interaction of a short, 9-residue peptide TK9 (T<sup>55</sup>VYVYSRVK<sup>63</sup>) that had been derived from the carboxyl terminal of the Severe Acute Respiratory Syndrome (SARS) corona virus (SARS CoV) envelope (E) protein. The peptide has been studied for its physical changes in the presence of both zwitterionic DPC and negatively charged SDS model membrane micelles, respectively, with the help of a battery of biophysical techniques including two-dimensional solution state NMR spectroscopy. Interestingly, in both micellar environments, TK9 adopted an alpha helical conformation; however, the helical propensities were much higher in the case of DPC compared to those of SDS micelle, suggesting that TK9 has more specificity towards eukaryotic cell membrane than the bacterial cell membrane. The orientation of the peptide TK9 also varies in the different micellar environments. The peptide's affinity was further manifested by its pronounced membrane disruption ability towards the mammalian compared to the bacterial membrane mimic. Collectively, the in-depth structural information on the interaction of TK9 with different membrane environments explains the host specificity and membrane orientation owing to subsequent membrane disruption implicated in the viral pathogenesis.</AbstractText><CopyrightInformation>Copyright © 2017 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ghosh</LastName><ForeName>Anirban</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bhattacharyya</LastName><ForeName>Dipita</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bhunia</LastName><ForeName>Anirban</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India. Electronic address: bhunia@jcbose.ac.in.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>10</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Biomembr</MedlineTA><NlmUniqueID>101731713</NlmUniqueID><ISSNLinking>0005-2736</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C501689">E protein, SARS coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008051">Lipid Bilayers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008823">Micelles</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009842">Oligopeptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D053835">Unilamellar Liposomes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>107-73-3</RegistryNumber><NameOfSubstance UI="D010767">Phosphorylcholine</NameOfSubstance></Chemical><Chemical><RegistryNumber>368GB5141J</RegistryNumber><NameOfSubstance UI="D012967">Sodium Dodecyl Sulfate</NameOfSubstance></Chemical><Chemical><RegistryNumber>53949-18-1</RegistryNumber><NameOfSubstance UI="C028810">dodecylphosphocholine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008051" MajorTopicYN="N">Lipid Bilayers</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008823" MajorTopicYN="Y">Micelles</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009842" MajorTopicYN="N">Oligopeptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010767" MajorTopicYN="N">Phosphorylcholine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012967" MajorTopicYN="N">Sodium Dodecyl Sulfate</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053835" MajorTopicYN="N">Unilamellar Liposomes</DescriptorName><QualifierName UI="Q000737" 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