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 : 000691 ( Main/Exploration ); précédent : 000690; suivant : 000692Structural 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 [Inde] ; Dipita Bhattacharyya [Inde] ; Anirban Bhunia [Inde]Source :
- Biochimica et biophysica acta. Biomembranes [ 0005-2736 ] ; 2018.
Descripteurs français
- KwdFr :
- Animaux, Dichroïsme circulaire, Dodécyl-sulfate de sodium (), Double couche lipidique (), Double couche lipidique (métabolisme), Humains, Liaison aux protéines, Liposomes unilamellaires (), Liposomes unilamellaires (métabolisme), Micelles, Modèles moléculaires, Oligopeptides (), Oligopeptides (métabolisme), Phosphoryl-choline (), Phosphoryl-choline (analogues et dérivés), Protéines de l'enveloppe virale (), Spectroscopie par résonance magnétique, Structure secondaire des protéines, Séquence d'acides aminés.
- MESH :
- analogues et dérivés : Phosphoryl-choline.
- métabolisme : Double couche lipidique, Liposomes unilamellaires, Oligopeptides.
- Animaux, Dichroïsme circulaire, Dodécyl-sulfate de sodium, Double couche lipidique, Humains, Liaison aux protéines, Liposomes unilamellaires, Micelles, Modèles moléculaires, Oligopeptides, Phosphoryl-choline, Protéines de l'enveloppe virale, Spectroscopie par résonance magnétique, Structure secondaire des protéines, Séquence d'acides aminés.
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
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 000606
- to stream PubMed, to step Curation: 000606
- to stream PubMed, to step Checkpoint: 000600
- to stream Ncbi, to step Merge: 000665
- to stream Ncbi, to step Curation: 000665
- to stream Ncbi, to step Checkpoint: 000665
- to stream Main, to step Merge: 000693
- to stream Main, to step Curation: 000691
Le 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 wicri:level="1"><nlm:affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054</wicri:regionArea><wicri:noRegion>Kolkata 700054</wicri:noRegion></affiliation></author><author><name sortKey="Bhattacharyya, Dipita" sort="Bhattacharyya, Dipita" uniqKey="Bhattacharyya D" first="Dipita" last="Bhattacharyya">Dipita Bhattacharyya</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054</wicri:regionArea><wicri:noRegion>Kolkata 700054</wicri:noRegion></affiliation></author><author><name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</name><affiliation wicri:level="1"><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><country xml:lang="fr">Inde</country><wicri:regionArea>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054</wicri:regionArea><wicri:noRegion>Kolkata 700054</wicri:noRegion></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><idno type="wicri:Area/PubMed/Curation">000606</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000606</idno><idno type="wicri:Area/PubMed/Checkpoint">000600</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000600</idno><idno type="wicri:Area/Ncbi/Merge">000665</idno><idno type="wicri:Area/Ncbi/Curation">000665</idno><idno type="wicri:Area/Ncbi/Checkpoint">000665</idno><idno type="wicri:doubleKey">0005-2736:2018:Ghosh A:structural:insights:of</idno><idno type="wicri:Area/Main/Merge">000693</idno><idno type="wicri:Area/Main/Curation">000691</idno><idno type="wicri:Area/Main/Exploration">000691</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 wicri:level="1"><nlm:affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054</wicri:regionArea><wicri:noRegion>Kolkata 700054</wicri:noRegion></affiliation></author><author><name sortKey="Bhattacharyya, Dipita" sort="Bhattacharyya, Dipita" uniqKey="Bhattacharyya D" first="Dipita" last="Bhattacharyya">Dipita Bhattacharyya</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054</wicri:regionArea><wicri:noRegion>Kolkata 700054</wicri:noRegion></affiliation></author><author><name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</name><affiliation wicri:level="1"><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><country xml:lang="fr">Inde</country><wicri:regionArea>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054</wicri:regionArea><wicri:noRegion>Kolkata 700054</wicri:noRegion></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="KwdFr" xml:lang="fr"><term>Animaux</term><term>Dichroïsme circulaire</term><term>Dodécyl-sulfate de sodium ()</term><term>Double couche lipidique ()</term><term>Double couche lipidique (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Liposomes unilamellaires ()</term><term>Liposomes unilamellaires (métabolisme)</term><term>Micelles</term><term>Modèles moléculaires</term><term>Oligopeptides ()</term><term>Oligopeptides (métabolisme)</term><term>Phosphoryl-choline ()</term><term>Phosphoryl-choline (analogues et dérivés)</term><term>Protéines de l'enveloppe virale ()</term><term>Spectroscopie par résonance magnétique</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</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" qualifier="analogues et dérivés" xml:lang="fr"><term>Phosphoryl-choline</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Double couche lipidique</term><term>Liposomes unilamellaires</term><term>Oligopeptides</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><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Dichroïsme circulaire</term><term>Dodécyl-sulfate de sodium</term><term>Double couche lipidique</term><term>Humains</term><term>Liaison aux protéines</term><term>Liposomes unilamellaires</term><term>Micelles</term><term>Modèles moléculaires</term><term>Oligopeptides</term><term>Phosphoryl-choline</term><term>Protéines de l'enveloppe virale</term><term>Spectroscopie par résonance magnétique</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</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><affiliations><list><country><li>Inde</li></country></list><tree><country name="Inde"><noRegion><name sortKey="Ghosh, Anirban" sort="Ghosh, Anirban" uniqKey="Ghosh A" first="Anirban" last="Ghosh">Anirban Ghosh</name></noRegion><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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/CovidV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000691 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000691 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Sante
|area= CovidV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:29038024
|texte= 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.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:29038024" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a CovidV1
| This area was generated with Dilib version V0.6.33. |  |