Membrane Cholesterol Modulates Oligomeric Status and Peptide-Membrane Interaction of Severe Acute Respiratory Syndrome Coronavirus Fusion Peptide.
Identifieur interne : 000B12 ( Main/Curation ); précédent : 000B11; suivant : 000B13Membrane Cholesterol Modulates Oligomeric Status and Peptide-Membrane Interaction of Severe Acute Respiratory Syndrome Coronavirus Fusion Peptide.
Auteurs : Geetanjali Meher [Inde] ; Surajit Bhattacharjya ; Hirak Chakraborty [Inde]Source :
- The journal of physical chemistry. B [ 1520-5207 ] ; 2019.
Abstract
The N-terminal fusion peptide (residues 770-788) of an S2 glycoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV), exposed upon receptor binding, is crucial for virus entry into the host cell. The fusion peptide alters the membrane organization and dynamics of the host membrane to facilitate membrane fusion. Generally, the effect of the fusion peptide on the membrane is sensitive to the lipid composition of target membranes. In the present work, we have utilized steady-state and time-resolved fluorescence spectroscopy in tandem with circular dichroism spectroscopy to elucidate the binding, oligomeric status, and secondary structure of the fusion peptide and its impact on the depth-dependent membrane organization and dynamics. We have used depth-dependent fluorescence probes, 1,6-diphenyl-1,3,5-hexatriene (DPH) and its trimethylammonium derivative (TMA-DPH), to evaluate the effect of the peptide binding along the bilayer normal. We have exploited the energy transfer efficiency of tryptophan between TMA-DPH and DPH to determine the relative location of the solitary tryptophan present in the membrane-bound fusion peptide. We have further evaluated the effect of membrane cholesterol on the binding and organization of the peptide and the impact of peptide binding on the depth-dependent physical properties of the membrane at various cholesterol concentrations. Our results clearly demonstrate that the membrane cholesterol alters the oligomeric status of the membrane-bound peptide and the effect of peptide binding on the depth-dependent membrane organization and dynamics. The role of cholesterol is important, as the eukaryotic host cells contain a good amount of cholesterol that might be important for the entry of pathogenic viruses.
DOI: 10.1021/acs.jpcb.9b08455
PubMed: 31743644
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000859
- to stream PubMed, to step Curation: Pour aller vers cette notice dans l'étape Curation :000859
- to stream PubMed, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :000881
- to stream Ncbi, to step Merge: Pour aller vers cette notice dans l'étape Curation :003103
- to stream Ncbi, to step Curation: Pour aller vers cette notice dans l'étape Curation :003103
- to stream Ncbi, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :003103
- to stream Main, to step Merge: Pour aller vers cette notice dans l'étape Curation :000B13
Links to Exploration step
pubmed:31743644Curation
No country items
Surajit Bhattacharjya<affiliation><nlm:affiliation>School of Biological Sciences , Nanyang Technological University , 60 Nanyang Drive , Singapore 637551.</nlm:affiliation><wicri:noCountry code="subField">Singapore 637551</wicri:noCountry></affiliation>Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Membrane Cholesterol Modulates Oligomeric Status and Peptide-Membrane Interaction of Severe Acute Respiratory Syndrome Coronavirus Fusion Peptide.</title><author><name sortKey="Meher, Geetanjali" sort="Meher, Geetanjali" uniqKey="Meher G" first="Geetanjali" last="Meher">Geetanjali Meher</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry , Sambalpur University , Jyoti Vihar , Burla , Odisha 768 019 , India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>School of Chemistry , Sambalpur University , Jyoti Vihar , Burla , Odisha 768 019 </wicri:regionArea><wicri:noRegion>Odisha 768 019 </wicri:noRegion></affiliation></author><author><name sortKey="Bhattacharjya, Surajit" sort="Bhattacharjya, Surajit" uniqKey="Bhattacharjya S" first="Surajit" last="Bhattacharjya">Surajit Bhattacharjya</name><affiliation><nlm:affiliation>School of Biological Sciences , Nanyang Technological University , 60 Nanyang Drive , Singapore 637551.</nlm:affiliation><wicri:noCountry code="subField">Singapore 637551</wicri:noCountry></affiliation></author><author><name sortKey="Chakraborty, Hirak" sort="Chakraborty, Hirak" uniqKey="Chakraborty H" first="Hirak" last="Chakraborty">Hirak Chakraborty</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry , Sambalpur University , Jyoti Vihar , Burla , Odisha 768 019 , India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>School of Chemistry , Sambalpur University , Jyoti Vihar , Burla , Odisha 768 019 </wicri:regionArea><wicri:noRegion>Odisha 768 019 </wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2019">2019</date><idno type="RBID">pubmed:31743644</idno><idno type="pmid">31743644</idno><idno type="doi">10.1021/acs.jpcb.9b08455</idno><idno type="wicri:Area/PubMed/Corpus">000859</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000859</idno><idno type="wicri:Area/PubMed/Curation">000859</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000859</idno><idno type="wicri:Area/PubMed/Checkpoint">000881</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000881</idno><idno type="wicri:Area/Ncbi/Merge">003103</idno><idno type="wicri:Area/Ncbi/Curation">003103</idno><idno type="wicri:Area/Ncbi/Checkpoint">003103</idno><idno type="wicri:Area/Main/Merge">000B13</idno><idno type="wicri:Area/Main/Curation">000B12</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Membrane Cholesterol Modulates Oligomeric Status and Peptide-Membrane Interaction of Severe Acute Respiratory Syndrome Coronavirus Fusion Peptide.</title><author><name sortKey="Meher, Geetanjali" sort="Meher, Geetanjali" uniqKey="Meher G" first="Geetanjali" last="Meher">Geetanjali Meher</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry , Sambalpur University , Jyoti Vihar , Burla , Odisha 768 019 , India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>School of Chemistry , Sambalpur University , Jyoti Vihar , Burla , Odisha 768 019 </wicri:regionArea><wicri:noRegion>Odisha 768 019 </wicri:noRegion></affiliation></author><author><name sortKey="Bhattacharjya, Surajit" sort="Bhattacharjya, Surajit" uniqKey="Bhattacharjya S" first="Surajit" last="Bhattacharjya">Surajit Bhattacharjya</name><affiliation><nlm:affiliation>School of Biological Sciences , Nanyang Technological University , 60 Nanyang Drive , Singapore 637551.</nlm:affiliation><wicri:noCountry code="subField">Singapore 637551</wicri:noCountry></affiliation></author><author><name sortKey="Chakraborty, Hirak" sort="Chakraborty, Hirak" uniqKey="Chakraborty H" first="Hirak" last="Chakraborty">Hirak Chakraborty</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry , Sambalpur University , Jyoti Vihar , Burla , Odisha 768 019 , India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>School of Chemistry , Sambalpur University , Jyoti Vihar , Burla , Odisha 768 019 </wicri:regionArea><wicri:noRegion>Odisha 768 019 </wicri:noRegion></affiliation></author></analytic><series><title level="j">The journal of physical chemistry. B</title><idno type="eISSN">1520-5207</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The N-terminal fusion peptide (residues 770-788) of an S2 glycoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV), exposed upon receptor binding, is crucial for virus entry into the host cell. The fusion peptide alters the membrane organization and dynamics of the host membrane to facilitate membrane fusion. Generally, the effect of the fusion peptide on the membrane is sensitive to the lipid composition of target membranes. In the present work, we have utilized steady-state and time-resolved fluorescence spectroscopy in tandem with circular dichroism spectroscopy to elucidate the binding, oligomeric status, and secondary structure of the fusion peptide and its impact on the depth-dependent membrane organization and dynamics. We have used depth-dependent fluorescence probes, 1,6-diphenyl-1,3,5-hexatriene (DPH) and its trimethylammonium derivative (TMA-DPH), to evaluate the effect of the peptide binding along the bilayer normal. We have exploited the energy transfer efficiency of tryptophan between TMA-DPH and DPH to determine the relative location of the solitary tryptophan present in the membrane-bound fusion peptide. We have further evaluated the effect of membrane cholesterol on the binding and organization of the peptide and the impact of peptide binding on the depth-dependent physical properties of the membrane at various cholesterol concentrations. Our results clearly demonstrate that the membrane cholesterol alters the oligomeric status of the membrane-bound peptide and the effect of peptide binding on the depth-dependent membrane organization and dynamics. The role of cholesterol is important, as the eukaryotic host cells contain a good amount of cholesterol that might be important for the entry of pathogenic viruses.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Main/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000B12 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Curation/biblio.hfd -nk 000B12 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= Main
|étape= Curation
|type= RBID
|clé= pubmed:31743644
|texte= Membrane Cholesterol Modulates Oligomeric Status and Peptide-Membrane Interaction of Severe Acute Respiratory Syndrome Coronavirus Fusion Peptide.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Curation/RBID.i -Sk "pubmed:31743644" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Curation/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |