Interaction of a peptide corresponding to the loop domain of the S2 SARS-CoV virus protein with model membranes.
Identifieur interne : 001912 ( PubMed/Corpus ); précédent : 001911; suivant : 001913Interaction of a peptide corresponding to the loop domain of the S2 SARS-CoV virus protein with model membranes.
Auteurs : Jaime Guillén ; Rodrigo F M. De Almeida ; Manuel Prieto ; José VillalaínSource :
- Molecular membrane biology [ 1464-5203 ] ; 2009.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Liposomes, Membrane Glycoproteins, Peptides, Phospholipids, Viral Envelope Proteins.
- physiology : Membrane Fusion.
- Spectrophotometry, Infrared, Spike Glycoprotein, Coronavirus.
Abstract
The severe acute respiratory syndrome coronavirus (SARS-CoV) envelope spike (S) glycoprotein is responsible for the fusion between the membranes of the virus and the target cell. In the case of the S2 domain of protein S, it has been found a highly hydrophobic and interfacial domain flanked by the heptad repeat 1 and 2 regions; significantly, different peptides pertaining to this domain have shown a significant leakage effect and an important plaque formation inhibition, which, similarly to HIV-1 gp41, support the role of this region in the fusion process. Therefore, we have carried out a study of the binding and interaction with model membranes of a peptide corresponding to segment 1073-1095 of the SARS-CoV S glycoprotein, peptide SARS(L) in the presence of different membrane model systems, as well as the structural changes taking place in both the lipid and the peptide induced by the binding of the peptide to the membrane. Our results show that SARS(L) strongly partitions into phospholipid membranes and organizes differently in lipid environments, displaying membrane activity modulated by the lipid composition of the membrane. These data would support its role in SARS-CoV mediated membrane fusion and suggest that the region where this peptide resides could be involved in the merging of the viral and target cell membranes.
DOI: 10.1080/09687680902926203
PubMed: 19412834
Links to Exploration step
pubmed:19412834Le document en format XML
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De Almeida</name></author><author><name sortKey="Prieto, Manuel" sort="Prieto, Manuel" uniqKey="Prieto M" first="Manuel" last="Prieto">Manuel Prieto</name></author><author><name sortKey="Villalain, Jose" sort="Villalain, Jose" uniqKey="Villalain J" first="José" last="Villalaín">José Villalaín</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19412834</idno><idno type="pmid">19412834</idno><idno type="doi">10.1080/09687680902926203</idno><idno type="wicri:Area/PubMed/Corpus">001912</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001912</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Interaction of a peptide corresponding to the loop domain of the S2 SARS-CoV virus protein with model membranes.</title><author><name sortKey="Guillen, Jaime" sort="Guillen, Jaime" uniqKey="Guillen J" first="Jaime" last="Guillén">Jaime Guillén</name><affiliation><nlm:affiliation>Instituto de Biologia Molecular y Celular, Universidad Miguel Hernandez, Elche-Alicante, Spain.</nlm:affiliation></affiliation></author><author><name sortKey="De Almeida, Rodrigo F M" sort="De Almeida, Rodrigo F M" uniqKey="De Almeida R" first="Rodrigo F M" last="De Almeida">Rodrigo F M. De Almeida</name></author><author><name sortKey="Prieto, Manuel" sort="Prieto, Manuel" uniqKey="Prieto M" first="Manuel" last="Prieto">Manuel Prieto</name></author><author><name sortKey="Villalain, Jose" sort="Villalain, Jose" uniqKey="Villalain J" first="José" last="Villalaín">José Villalaín</name></author></analytic><series><title level="j">Molecular membrane biology</title><idno type="eISSN">1464-5203</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Liposomes (chemistry)</term><term>Membrane Fusion (physiology)</term><term>Membrane Glycoproteins (chemistry)</term><term>Peptides (chemistry)</term><term>Phospholipids (chemistry)</term><term>Spectrophotometry, Infrared</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Liposomes</term><term>Membrane Glycoproteins</term><term>Peptides</term><term>Phospholipids</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Membrane Fusion</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Spectrophotometry, Infrared</term><term>Spike Glycoprotein, Coronavirus</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV) envelope spike (S) glycoprotein is responsible for the fusion between the membranes of the virus and the target cell. In the case of the S2 domain of protein S, it has been found a highly hydrophobic and interfacial domain flanked by the heptad repeat 1 and 2 regions; significantly, different peptides pertaining to this domain have shown a significant leakage effect and an important plaque formation inhibition, which, similarly to HIV-1 gp41, support the role of this region in the fusion process. Therefore, we have carried out a study of the binding and interaction with model membranes of a peptide corresponding to segment 1073-1095 of the SARS-CoV S glycoprotein, peptide SARS(L) in the presence of different membrane model systems, as well as the structural changes taking place in both the lipid and the peptide induced by the binding of the peptide to the membrane. Our results show that SARS(L) strongly partitions into phospholipid membranes and organizes differently in lipid environments, displaying membrane activity modulated by the lipid composition of the membrane. These data would support its role in SARS-CoV mediated membrane fusion and suggest that the region where this peptide resides could be involved in the merging of the viral and target cell membranes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19412834</PMID><DateCompleted><Year>2009</Year><Month>07</Month><Day>21</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>03</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1464-5203</ISSN><JournalIssue CitedMedium="Internet"><Volume>26</Volume><Issue>4</Issue><PubDate><Year>2009</Year><Month>May</Month></PubDate></JournalIssue><Title>Molecular membrane biology</Title><ISOAbbreviation>Mol. Membr. Biol.</ISOAbbreviation></Journal><ArticleTitle>Interaction of a peptide corresponding to the loop domain of the S2 SARS-CoV virus protein with model membranes.</ArticleTitle><Pagination><MedlinePgn>236-48</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1080/09687680902926203</ELocationID><Abstract><AbstractText>The severe acute respiratory syndrome coronavirus (SARS-CoV) envelope spike (S) glycoprotein is responsible for the fusion between the membranes of the virus and the target cell. In the case of the S2 domain of protein S, it has been found a highly hydrophobic and interfacial domain flanked by the heptad repeat 1 and 2 regions; significantly, different peptides pertaining to this domain have shown a significant leakage effect and an important plaque formation inhibition, which, similarly to HIV-1 gp41, support the role of this region in the fusion process. Therefore, we have carried out a study of the binding and interaction with model membranes of a peptide corresponding to segment 1073-1095 of the SARS-CoV S glycoprotein, peptide SARS(L) in the presence of different membrane model systems, as well as the structural changes taking place in both the lipid and the peptide induced by the binding of the peptide to the membrane. Our results show that SARS(L) strongly partitions into phospholipid membranes and organizes differently in lipid environments, displaying membrane activity modulated by the lipid composition of the membrane. These data would support its role in SARS-CoV mediated membrane fusion and suggest that the region where this peptide resides could be involved in the merging of the viral and target cell membranes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Guillén</LastName><ForeName>Jaime</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Instituto de Biologia Molecular y Celular, Universidad Miguel Hernandez, Elche-Alicante, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>De Almeida</LastName><ForeName>Rodrigo F M</ForeName><Initials>RF</Initials></Author><Author ValidYN="Y"><LastName>Prieto</LastName><ForeName>Manuel</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Villalaín</LastName><ForeName>José</ForeName><Initials>J</Initials></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>2009</Year><Month>04</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Mol Membr Biol</MedlineTA><NlmUniqueID>9430797</NlmUniqueID><ISSNLinking>0968-7688</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008081">Liposomes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010743">Phospholipids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, 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