SARS-CoV fusion peptides induce membrane surface ordering and curvature.
Identifieur interne : 000B85 ( PubMed/Corpus ); précédent : 000B84; suivant : 000B86SARS-CoV fusion peptides induce membrane surface ordering and curvature.
Auteurs : Luis G M. Basso ; Eduardo F. Vicente ; Edson Crusca ; Eduardo M. Cilli ; Antonio J. Costa-FilhoSource :
- Scientific reports [ 2045-2322 ] ; 2016.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Peptides, Viral Fusion Proteins.
- chemistry : Cell Membrane, SARS Virus.
- Calorimetry, Differential Scanning, Electron Spin Resonance Spectroscopy, Membrane Fusion, Thermodynamics, Virus Internalization.
Abstract
Viral membrane fusion is an orchestrated process triggered by membrane-anchored viral fusion glycoproteins. The S2 subunit of the spike glycoprotein from severe acute respiratory syndrome (SARS) coronavirus (CoV) contains internal domains called fusion peptides (FP) that play essential roles in virus entry. Although membrane fusion has been broadly studied, there are still major gaps in the molecular details of lipid rearrangements in the bilayer during fusion peptide-membrane interactions. Here we employed differential scanning calorimetry (DSC) and electron spin resonance (ESR) to gather information on the membrane fusion mechanism promoted by two putative SARS FPs. DSC data showed the peptides strongly perturb the structural integrity of anionic vesicles and support the hypothesis that the peptides generate opposing curvature stresses on phosphatidylethanolamine membranes. ESR showed that both FPs increase lipid packing and head group ordering as well as reduce the intramembrane water content for anionic membranes. Therefore, bending moment in the bilayer could be generated, promoting negative curvature. The significance of the ordering effect, membrane dehydration, changes in the curvature properties and the possible role of negatively charged phospholipids in helping to overcome the high kinetic barrier involved in the different stages of the SARS-CoV-mediated membrane fusion are discussed.
DOI: 10.1038/srep37131
PubMed: 27892522
Links to Exploration step
pubmed:27892522Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">SARS-CoV fusion peptides induce membrane surface ordering and curvature.</title><author><name sortKey="Basso, Luis G M" sort="Basso, Luis G M" uniqKey="Basso L" first="Luis G M" last="Basso">Luis G M. Basso</name><affiliation><nlm:affiliation>Grupo de Biofísica Molecular Sérgio Mascarenhas, Instituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São-carlense, 400, Centro, São Carlos, SP, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Vicente, Eduardo F" sort="Vicente, Eduardo F" uniqKey="Vicente E" first="Eduardo F" last="Vicente">Eduardo F. Vicente</name><affiliation><nlm:affiliation>Faculdade de Ciências e Engenharia, UNESP - Univ Estadual Paulista, Campus de Tupã. Rua Domingos da Costa Lopes, 780, 17602-496, Tupã, SP, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Crusca, Edson" sort="Crusca, Edson" uniqKey="Crusca E" first="Edson" last="Crusca">Edson Crusca</name><affiliation><nlm:affiliation>Departamento de Bioquímica e Tecnologia Química, Instituto de Química, UNESP - Univ Estadual Paulista. Rua Prof. Franscisco Degni, 55, 14800-900, Araraquara, SP, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Cilli, Eduardo M" sort="Cilli, Eduardo M" uniqKey="Cilli E" first="Eduardo M" last="Cilli">Eduardo M. Cilli</name><affiliation><nlm:affiliation>Departamento de Bioquímica e Tecnologia Química, Instituto de Química, UNESP - Univ Estadual Paulista. Rua Prof. Franscisco Degni, 55, 14800-900, Araraquara, SP, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Costa Filho, Antonio J" sort="Costa Filho, Antonio J" uniqKey="Costa Filho A" first="Antonio J" last="Costa-Filho">Antonio J. Costa-Filho</name><affiliation><nlm:affiliation>Laboratório de Biofísica Molecular, Departamento de Física, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo. Av. Bandeirantes, 3900, 14040-901, Ribeirão Preto, SP, Brazil.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:27892522</idno><idno type="pmid">27892522</idno><idno type="doi">10.1038/srep37131</idno><idno type="wicri:Area/PubMed/Corpus">000B85</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000B85</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">SARS-CoV fusion peptides induce membrane surface ordering and curvature.</title><author><name sortKey="Basso, Luis G M" sort="Basso, Luis G M" uniqKey="Basso L" first="Luis G M" last="Basso">Luis G M. Basso</name><affiliation><nlm:affiliation>Grupo de Biofísica Molecular Sérgio Mascarenhas, Instituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São-carlense, 400, Centro, São Carlos, SP, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Vicente, Eduardo F" sort="Vicente, Eduardo F" uniqKey="Vicente E" first="Eduardo F" last="Vicente">Eduardo F. Vicente</name><affiliation><nlm:affiliation>Faculdade de Ciências e Engenharia, UNESP - Univ Estadual Paulista, Campus de Tupã. Rua Domingos da Costa Lopes, 780, 17602-496, Tupã, SP, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Crusca, Edson" sort="Crusca, Edson" uniqKey="Crusca E" first="Edson" last="Crusca">Edson Crusca</name><affiliation><nlm:affiliation>Departamento de Bioquímica e Tecnologia Química, Instituto de Química, UNESP - Univ Estadual Paulista. Rua Prof. Franscisco Degni, 55, 14800-900, Araraquara, SP, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Cilli, Eduardo M" sort="Cilli, Eduardo M" uniqKey="Cilli E" first="Eduardo M" last="Cilli">Eduardo M. Cilli</name><affiliation><nlm:affiliation>Departamento de Bioquímica e Tecnologia Química, Instituto de Química, UNESP - Univ Estadual Paulista. Rua Prof. Franscisco Degni, 55, 14800-900, Araraquara, SP, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Costa Filho, Antonio J" sort="Costa Filho, Antonio J" uniqKey="Costa Filho A" first="Antonio J" last="Costa-Filho">Antonio J. Costa-Filho</name><affiliation><nlm:affiliation>Laboratório de Biofísica Molecular, Departamento de Física, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo. Av. Bandeirantes, 3900, 14040-901, Ribeirão Preto, SP, Brazil.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Calorimetry, Differential Scanning</term><term>Cell Membrane (chemistry)</term><term>Electron Spin Resonance Spectroscopy</term><term>Membrane Fusion</term><term>Peptides (chemistry)</term><term>SARS Virus (chemistry)</term><term>Thermodynamics</term><term>Viral Fusion Proteins (chemistry)</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptides</term><term>Viral Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Membrane</term><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Calorimetry, Differential Scanning</term><term>Electron Spin Resonance Spectroscopy</term><term>Membrane Fusion</term><term>Thermodynamics</term><term>Virus Internalization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Viral membrane fusion is an orchestrated process triggered by membrane-anchored viral fusion glycoproteins. The S2 subunit of the spike glycoprotein from severe acute respiratory syndrome (SARS) coronavirus (CoV) contains internal domains called fusion peptides (FP) that play essential roles in virus entry. Although membrane fusion has been broadly studied, there are still major gaps in the molecular details of lipid rearrangements in the bilayer during fusion peptide-membrane interactions. Here we employed differential scanning calorimetry (DSC) and electron spin resonance (ESR) to gather information on the membrane fusion mechanism promoted by two putative SARS FPs. DSC data showed the peptides strongly perturb the structural integrity of anionic vesicles and support the hypothesis that the peptides generate opposing curvature stresses on phosphatidylethanolamine membranes. ESR showed that both FPs increase lipid packing and head group ordering as well as reduce the intramembrane water content for anionic membranes. Therefore, bending moment in the bilayer could be generated, promoting negative curvature. The significance of the ordering effect, membrane dehydration, changes in the curvature properties and the possible role of negatively charged phospholipids in helping to overcome the high kinetic barrier involved in the different stages of the SARS-CoV-mediated membrane fusion are discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27892522</PMID><DateCompleted><Year>2018</Year><Month>05</Month><Day>14</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>15</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>6</Volume><PubDate><Year>2016</Year><Month>11</Month><Day>28</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>SARS-CoV fusion peptides induce membrane surface ordering and curvature.</ArticleTitle><Pagination><MedlinePgn>37131</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/srep37131</ELocationID><Abstract><AbstractText>Viral membrane fusion is an orchestrated process triggered by membrane-anchored viral fusion glycoproteins. The S2 subunit of the spike glycoprotein from severe acute respiratory syndrome (SARS) coronavirus (CoV) contains internal domains called fusion peptides (FP) that play essential roles in virus entry. Although membrane fusion has been broadly studied, there are still major gaps in the molecular details of lipid rearrangements in the bilayer during fusion peptide-membrane interactions. Here we employed differential scanning calorimetry (DSC) and electron spin resonance (ESR) to gather information on the membrane fusion mechanism promoted by two putative SARS FPs. DSC data showed the peptides strongly perturb the structural integrity of anionic vesicles and support the hypothesis that the peptides generate opposing curvature stresses on phosphatidylethanolamine membranes. ESR showed that both FPs increase lipid packing and head group ordering as well as reduce the intramembrane water content for anionic membranes. Therefore, bending moment in the bilayer could be generated, promoting negative curvature. The significance of the ordering effect, membrane dehydration, changes in the curvature properties and the possible role of negatively charged phospholipids in helping to overcome the high kinetic barrier involved in the different stages of the SARS-CoV-mediated membrane fusion are discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Basso</LastName><ForeName>Luis G M</ForeName><Initials>LG</Initials><AffiliationInfo><Affiliation>Grupo de Biofísica Molecular Sérgio Mascarenhas, Instituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São-carlense, 400, Centro, São Carlos, SP, Brazil.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Laboratório de Biofísica Molecular, Departamento de Física, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo. Av. Bandeirantes, 3900, 14040-901, Ribeirão Preto, SP, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vicente</LastName><ForeName>Eduardo F</ForeName><Initials>EF</Initials><AffiliationInfo><Affiliation>Faculdade de Ciências e Engenharia, UNESP - Univ Estadual Paulista, Campus de Tupã. Rua Domingos da Costa Lopes, 780, 17602-496, Tupã, SP, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Crusca</LastName><ForeName>Edson</ForeName><Initials>E</Initials><Suffix>Jr</Suffix><AffiliationInfo><Affiliation>Departamento de Bioquímica e Tecnologia Química, Instituto de Química, UNESP - Univ Estadual Paulista. Rua Prof. Franscisco Degni, 55, 14800-900, Araraquara, SP, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cilli</LastName><ForeName>Eduardo M</ForeName><Initials>EM</Initials><AffiliationInfo><Affiliation>Departamento de Bioquímica e Tecnologia Química, Instituto de Química, UNESP - Univ Estadual Paulista. Rua Prof. Franscisco Degni, 55, 14800-900, Araraquara, SP, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Costa-Filho</LastName><ForeName>Antonio J</ForeName><Initials>AJ</Initials><AffiliationInfo><Affiliation>Laboratório de Biofísica Molecular, Departamento de Física, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo. Av. 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