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 : 000582 ( Pmc/Checkpoint ); précédent : 000581; suivant : 000583Structural 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 ] ; 2017.
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.
Url:
DOI: 10.1016/j.bbamem.2017.10.015
PubMed: 29038024
PubMed Central: 7094419
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<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></author><author><name sortKey="Bhattacharyya, Dipita" sort="Bhattacharyya, Dipita" uniqKey="Bhattacharyya D" first="Dipita" last="Bhattacharyya">Dipita Bhattacharyya</name></author><author><name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">29038024</idno><idno type="pmc">7094419</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094419</idno><idno type="RBID">PMC:7094419</idno><idno type="doi">10.1016/j.bbamem.2017.10.015</idno><date when="2017">2017</date><idno type="wicri:Area/Pmc/Corpus">000E33</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000E33</idno><idno type="wicri:Area/Pmc/Curation">000E33</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000E33</idno><idno type="wicri:Area/Pmc/Checkpoint">000582</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000582</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">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></author><author><name sortKey="Bhattacharyya, Dipita" sort="Bhattacharyya, Dipita" uniqKey="Bhattacharyya D" first="Dipita" last="Bhattacharyya">Dipita Bhattacharyya</name></author><author><name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</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="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>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.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Peiris, J" uniqKey="Peiris J">J. Peiris</name></author><author><name sortKey="Lai, S" uniqKey="Lai S">S. Lai</name></author><author><name sortKey="Poon, L" uniqKey="Poon L">L. Poon</name></author><author><name sortKey="Guan, Y" uniqKey="Guan Y">Y. Guan</name></author><author><name sortKey="Yam, L" uniqKey="Yam L">L. Yam</name></author><author><name sortKey="Lim, W" uniqKey="Lim W">W. Lim</name></author><author><name sortKey="Nicholls, J" uniqKey="Nicholls J">J. Nicholls</name></author><author><name sortKey="Yee, W" uniqKey="Yee W">W. Yee</name></author><author><name sortKey="Yan, W" uniqKey="Yan W">W. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Biochim Biophys Acta Biomembr</journal-id><journal-id journal-id-type="iso-abbrev">Biochim Biophys Acta Biomembr</journal-id><journal-title-group><journal-title>Biochimica et Biophysica Acta. Biomembranes</journal-title></journal-title-group><issn pub-type="ppub">0005-2736</issn><issn pub-type="epub">1879-2642</issn><publisher><publisher-name>Elsevier B.V.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">29038024</article-id><article-id pub-id-type="pmc">7094419</article-id><article-id pub-id-type="publisher-id">S0005-2736(17)30333-4</article-id><article-id pub-id-type="doi">10.1016/j.bbamem.2017.10.015</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>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</article-title></title-group><contrib-group><contrib contrib-type="author" id="au0005"><name><surname>Ghosh</surname><given-names>Anirban</given-names></name></contrib><contrib contrib-type="author" id="au0010"><name><surname>Bhattacharyya</surname><given-names>Dipita</given-names></name></contrib><contrib contrib-type="author" id="au0015"><name><surname>Bhunia</surname><given-names>Anirban</given-names></name><email>bhunia@jcbose.ac.in</email><xref rid="cr0005" ref-type="corresp">⁎</xref></contrib></contrib-group><aff id="af0005">Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India</aff><author-notes><corresp id="cr0005"><label>⁎</label>Corresponding author. <email>bhunia@jcbose.ac.in</email></corresp></author-notes><pub-date pub-type="pmc-release"><day>14</day><month>10</month><year>2017</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><month>2</month><year>2018</year></pub-date><pub-date pub-type="epub"><day>14</day><month>10</month><year>2017</year></pub-date><volume>1860</volume><issue>2</issue><fpage>335</fpage><lpage>346</lpage><history><date date-type="received"><day>4</day><month>5</month><year>2017</year></date><date date-type="rev-recd"><day>9</day><month>10</month><year>2017</year></date><date date-type="accepted"><day>11</day><month>10</month><year>2017</year></date></history><permissions><copyright-statement>© 2017 Elsevier B.V.</copyright-statement><copyright-year>2017</copyright-year><copyright-holder>Elsevier B.V.</copyright-holder><license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p></license></permissions><abstract id="ab0005"><p>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.</p></abstract><abstract abstract-type="graphical" id="ab0010"><title>Graphical abstract</title><p><fig id="f0050" position="anchor"><alt-text id="al0055">Image 2</alt-text><graphic xlink:href="fx1_lrg"></graphic></fig></p></abstract><abstract abstract-type="author-highlights" id="ab0015"><title>Highlights</title><p><list list-type="simple" id="l0005"><list-item id="li0005"><label>•</label><p id="p0005">The study highlights membrane affinity of the short amyloidogenic sequence of TK9.</p></list-item><list-item id="li0010"><label>•</label><p id="p0010">The peptide adopts a helical conformation upon binding with membrane lipids.</p></list-item><list-item id="li0015"><label>•</label><p id="p0015">TK9 orients deeper into the zwitterionic lipids causing greater membrane disruption.</p></list-item><list-item id="li0020"><label>•</label><p id="p0020">Electrostatic interactions lead to a surfaced orientation for the anionic membranes.</p></list-item></list></p></abstract><kwd-group id="ks0005"><title>Abbreviations</title><kwd>SARS, Severe Acute Respiratory Syndrome</kwd><kwd>CoV, corona virus</kwd><kwd>ssRNA, single-stranded ribonucleic acid</kwd><kwd>TOCSY, total correlation spectroscopy</kwd><kwd>NOESY, nuclear overhauser effect spectroscopy</kwd><kwd>DSS, 4,4-dimethyl-4-silapentane-1-sulfonic acid</kwd><kwd>SDS, sodium dodecyl sulfate</kwd><kwd>DPC, dodecylphosphocholine</kwd><kwd>RMSD, root-mean-square deviation</kwd><kwd>HSQC, heteronuclear single-quantum correlation</kwd><kwd>CPMG, Carr-Purcell-Meiboom-Gill</kwd><kwd>DPH, 1,6-diphenyl-1,3,5-hexatriene</kwd><kwd>LUVs, large unilamellar vesicles</kwd><kwd>POPE, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine</kwd><kwd>POPG, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol</kwd></kwd-group><kwd-group id="ks0010"><title>Keywords</title><kwd>NMR</kwd><kwd>SARS CoV</kwd><kwd>Micelle</kwd><kwd>NOESY</kwd><kwd>Paramagnetic relaxation</kwd></kwd-group></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Bhattacharyya, Dipita" sort="Bhattacharyya, Dipita" uniqKey="Bhattacharyya D" first="Dipita" last="Bhattacharyya">Dipita Bhattacharyya</name><name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</name><name sortKey="Ghosh, Anirban" sort="Ghosh, Anirban" uniqKey="Ghosh A" first="Anirban" last="Ghosh">Anirban Ghosh</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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