NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion.
Identifieur interne : 000A73 ( PubMed/Corpus ); précédent : 000A72; suivant : 000A74NMR 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 ] ; 2018.
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.
DOI: 10.1016/j.bbamem.2017.10.002
PubMed: 28988778
Links to Exploration step
pubmed:28988778Le document en format XML
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Electronic address: surajit@ntu.edu.sg.</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>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="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="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" 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></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28988778</PMID><DateCompleted><Year>2018</Year><Month>05</Month><Day>22</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</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>NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion.</ArticleTitle><Pagination><MedlinePgn>407-415</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0005-2736(17)30312-7</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbamem.2017.10.002</ELocationID><Abstract><AbstractText>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.</AbstractText><CopyrightInformation>Copyright © 2017 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mahajan</LastName><ForeName>Mukesh</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chatterjee</LastName><ForeName>Deepak</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bhuvaneswari</LastName><ForeName>Kannaian</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pillay</LastName><ForeName>Shubhadra</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bhattacharjya</LastName><ForeName>Surajit</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore. Electronic address: surajit@ntu.edu.sg.</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>05</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="D008823">Micelles</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>107-73-3</RegistryNumber><NameOfSubstance UI="D010767">Phosphorylcholine</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="D057927" MajorTopicYN="N">Hydrophobic and Hydrophilic Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008561" MajorTopicYN="Y">Membrane Fusion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008823" MajorTopicYN="N">Micelles</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010767" MajorTopicYN="N">Phosphorylcholine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055672" MajorTopicYN="N">Static Electricity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053586" MajorTopicYN="Y">Virus Internalization</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Cell fusion</Keyword><Keyword MajorTopicYN="Y">Fusion peptide</Keyword><Keyword MajorTopicYN="Y">Fusion protein</Keyword><Keyword 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