NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion
Identifieur interne : 000C67 ( Main/Exploration ); précédent : 000C66; suivant : 000C68NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion
Auteurs : Mukesh Mahajan ; Deepak Chatterjee ; Kannaian Bhuvaneswari ; Shubhadra Pillay ; Surajit BhattacharjyaSource :
- Biochimica et Biophysica Acta. Biomembranes [ 0005-2736 ] ; 2017.
Descripteurs français
- KwdFr :
- Conformation des protéines, Fusion membranaire, Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (métabolisme), Interactions hydrophobes et hydrophiles, Liaison aux protéines, Micelles, Modèles moléculaires, Multimérisation de protéines, Peptides (), Peptides (métabolisme), Phosphoryl-choline (), Phosphoryl-choline (analogues et dérivés), Phosphoryl-choline (métabolisme), Pénétration virale, Spectroscopie par résonance magnétique (), Séquence d'acides aminés, Virus du SRAS (), Virus du SRAS (métabolisme), Électricité statique.
- MESH :
- analogues et dérivés : Phosphoryl-choline.
- métabolisme : Glycoprotéine de spicule des coronavirus, Peptides, Phosphoryl-choline, Virus du SRAS.
- Conformation des protéines, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Interactions hydrophobes et hydrophiles, Liaison aux protéines, Micelles, Modèles moléculaires, Multimérisation de protéines, Peptides, Phosphoryl-choline, Pénétration virale, Spectroscopie par résonance magnétique, Séquence d'acides aminés, Virus du SRAS, Électricité statique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Hydrophobic and Hydrophilic Interactions, Magnetic Resonance Spectroscopy (methods), Membrane Fusion, Micelles, Models, Molecular, Peptides (chemistry), Peptides (metabolism), Phosphorylcholine (analogs & derivatives), Phosphorylcholine (chemistry), Phosphorylcholine (metabolism), Protein Binding, Protein Conformation, Protein Multimerization, SARS Virus (chemistry), SARS Virus (metabolism), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (metabolism), Static Electricity, Virus Internalization.
- MESH :
- chemical , analogs & derivatives : Phosphorylcholine.
- chemical , chemistry : Peptides, Phosphorylcholine, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Peptides, Phosphorylcholine, Spike Glycoprotein, Coronavirus.
- chemical : Micelles.
- chemistry : SARS Virus.
- metabolism : SARS Virus.
- methods : Magnetic Resonance Spectroscopy.
- Amino Acid Sequence, Hydrophobic and Hydrophilic Interactions, Membrane Fusion, Models, Molecular, Protein Binding, Protein Conformation, Protein Multimerization, Static Electricity, Virus Internalization.
Abstract
The lethal Coronaviruses (CoVs), Severe Acute Respiratory Syndrome-associated Coronavirus (SARS-CoV) and most recently Middle East Respiratory Syndrome Coronavirus, (MERS-CoV) are serious human health hazard. A successful viral infection requires fusion between virus and host cells carried out by the surface spike glycoprotein or S protein of CoV. Current models propose that the S2 subunit of S protein assembled into a hexameric helical bundle exposing hydrophobic fusogenic peptides or fusion peptides (FPs) for membrane insertion. The N-terminus of S2 subunit of SARS-CoV reported to be active in cell fusion whereby FPs have been identified. Atomic-resolution structure of FPs derived either in model membranes or in membrane mimic environment would glean insights toward viral cell fusion mechanism. Here, we have solved 3D structure, dynamics and micelle localization of a 64-residue long fusion peptide or LFP in DPC detergent micelles by NMR methods. Micelle bound structure of LFP is elucidated by the presence of discretely folded helical and intervening loops. The C-terminus region, residues F42-Y62, displays a long hydrophobic helix, whereas the N-terminus is defined by a short amphipathic helix, residues R4-Q12. The intervening residues of LFP assume stretches of loops and helical turns. The N-terminal helix is sustained by close aromatic and aliphatic sidechain packing interactions at the non-polar face. 15N{1H}NOE studies indicated dynamical motion, at ps-ns timescale, of the helices of LFP in DPC micelles. PRE NMR showed that insertion of several regions of LFP into DPC micelle core. Together, the current study provides insights toward fusion mechanism of SARS-CoV.
Url:
DOI: 10.1016/j.bbamem.2017.10.002
PubMed: 28988778
PubMed Central: 7094225
Affiliations:
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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><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Magnetic Resonance Spectroscopy (methods)</term><term>Membrane Fusion</term><term>Micelles</term><term>Models, Molecular</term><term>Peptides (chemistry)</term><term>Peptides (metabolism)</term><term>Phosphorylcholine (analogs & derivatives)</term><term>Phosphorylcholine (chemistry)</term><term>Phosphorylcholine (metabolism)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>SARS Virus (chemistry)</term><term>SARS Virus (metabolism)</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Static Electricity</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus ()</term><term>Glycoprotéine de spicule des coronavirus (métabolisme)</term><term>Interactions hydrophobes et hydrophiles</term><term>Liaison aux protéines</term><term>Micelles</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Peptides ()</term><term>Peptides (métabolisme)</term><term>Phosphoryl-choline ()</term><term>Phosphoryl-choline (analogues et dérivés)</term><term>Phosphoryl-choline (métabolisme)</term><term>Pénétration virale</term><term>Spectroscopie par résonance magnétique ()</term><term>Séquence d'acides aminés</term><term>Virus du SRAS ()</term><term>Virus du SRAS (métabolisme)</term><term>Électricité statique</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>Peptides</term><term>Phosphorylcholine</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptides</term><term>Phosphorylcholine</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Micelles</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Phosphoryl-choline</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Magnetic Resonance Spectroscopy</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term><term>Peptides</term><term>Phosphoryl-choline</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Membrane Fusion</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>Static Electricity</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Interactions hydrophobes et hydrophiles</term><term>Liaison aux protéines</term><term>Micelles</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Peptides</term><term>Phosphoryl-choline</term><term>Pénétration virale</term><term>Spectroscopie par résonance magnétique</term><term>Séquence d'acides aminés</term><term>Virus du SRAS</term><term>Électricité statique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The lethal Coronaviruses (CoVs), Severe Acute Respiratory Syndrome-associated Coronavirus (SARS-CoV) and most recently Middle East Respiratory Syndrome Coronavirus, (MERS-CoV) are serious human health hazard. A successful viral infection requires fusion between virus and host cells carried out by the surface spike glycoprotein or S protein of CoV. Current models propose that the S2 subunit of S protein assembled into a hexameric helical bundle exposing hydrophobic fusogenic peptides or fusion peptides (FPs) for membrane insertion. The N-terminus of S2 subunit of SARS-CoV reported to be active in cell fusion whereby FPs have been identified. Atomic-resolution structure of FPs derived either in model membranes or in membrane mimic environment would glean insights toward viral cell fusion mechanism. Here, we have solved 3D structure, dynamics and micelle localization of a 64-residue long fusion peptide or LFP in DPC detergent micelles by NMR methods. Micelle bound structure of LFP is elucidated by the presence of discretely folded helical and intervening loops. The C-terminus region, residues F42-Y62, displays a long hydrophobic helix, whereas the N-terminus is defined by a short amphipathic helix, residues R4-Q12. The intervening residues of LFP assume stretches of loops and helical turns. The N-terminal helix is sustained by close aromatic and aliphatic sidechain packing interactions at the non-polar face. <sup>15</sup>N{<sup>1</sup>H}NOE studies indicated dynamical motion, at ps-ns timescale, of the helices of LFP in DPC micelles. PRE NMR showed that insertion of several regions of LFP into DPC micelle core. Together, the current study provides insights toward fusion mechanism of SARS-CoV.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Skehel, J J" uniqKey="Skehel J">J.J. Skehel</name></author><author><name sortKey="Wiley, D C" uniqKey="Wiley D">D.C. Wiley</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Eckert, D M" uniqKey="Eckert D">D.M. 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Lu</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Bhattacharjya, Surajit" sort="Bhattacharjya, Surajit" uniqKey="Bhattacharjya S" first="Surajit" last="Bhattacharjya">Surajit Bhattacharjya</name><name sortKey="Bhuvaneswari, Kannaian" sort="Bhuvaneswari, Kannaian" uniqKey="Bhuvaneswari K" first="Kannaian" last="Bhuvaneswari">Kannaian Bhuvaneswari</name><name sortKey="Chatterjee, Deepak" sort="Chatterjee, Deepak" uniqKey="Chatterjee D" first="Deepak" last="Chatterjee">Deepak Chatterjee</name><name sortKey="Mahajan, Mukesh" sort="Mahajan, Mukesh" uniqKey="Mahajan M" first="Mukesh" last="Mahajan">Mukesh Mahajan</name><name sortKey="Pillay, Shubhadra" sort="Pillay, Shubhadra" uniqKey="Pillay S" first="Shubhadra" last="Pillay">Shubhadra Pillay</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion
}}
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:28988778" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
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