SARS-CoV fusion peptides induce membrane surface ordering and curvature
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1038/srep37131 http://hdl.handle.net/11449/173854 |
Resumo: | 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. |
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SARS-CoV fusion peptides induce membrane surface ordering and curvatureViral 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.Grupo de Biofísica Molecular Sérgio Mascarenhas Instituto de Física de São Carlos Universidade de São Paulo, Avenida Trabalhador São-carlense, 400Departamento de Física Faculdade de Filosofia Ciências e Letras de Ribeirão Preto Universidade de São Paulo, Av. Bandeirantes, 3900Faculdade de Ciências e Engenharia UNESP - Univ Estadual Paulista Campus de Tupã, Rua Domingos da Costa Lopes, 780Departamento de Bioquímica e Tecnologia Química Instituto de Química UNESP - Univ Estadual Paulista, Rua Prof. Franscisco Degni, 55Faculdade de Ciências e Engenharia UNESP - Univ Estadual Paulista Campus de Tupã, Rua Domingos da Costa Lopes, 780Departamento de Bioquímica e Tecnologia Química Instituto de Química UNESP - Univ Estadual Paulista, Rua Prof. Franscisco Degni, 55Universidade de São Paulo (USP)Universidade Estadual Paulista (Unesp)Basso, Luis G.M.Vicente, Eduardo F. [UNESP]Crusca, Edson [UNESP]Cilli, Eduardo M. [UNESP]Costa-Filho, Antonio J.2018-12-11T17:08:03Z2018-12-11T17:08:03Z2016-11-28info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://dx.doi.org/10.1038/srep37131Scientific Reports, v. 6.2045-2322http://hdl.handle.net/11449/17385410.1038/srep371312-s2.0-849996635872-s2.0-84999663587.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengScientific Reports1,533info:eu-repo/semantics/openAccess2023-10-24T06:12:43Zoai:repositorio.unesp.br:11449/173854Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-10-24T06:12:43Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
SARS-CoV fusion peptides induce membrane surface ordering and curvature |
title |
SARS-CoV fusion peptides induce membrane surface ordering and curvature |
spellingShingle |
SARS-CoV fusion peptides induce membrane surface ordering and curvature Basso, Luis G.M. |
title_short |
SARS-CoV fusion peptides induce membrane surface ordering and curvature |
title_full |
SARS-CoV fusion peptides induce membrane surface ordering and curvature |
title_fullStr |
SARS-CoV fusion peptides induce membrane surface ordering and curvature |
title_full_unstemmed |
SARS-CoV fusion peptides induce membrane surface ordering and curvature |
title_sort |
SARS-CoV fusion peptides induce membrane surface ordering and curvature |
author |
Basso, Luis G.M. |
author_facet |
Basso, Luis G.M. Vicente, Eduardo F. [UNESP] Crusca, Edson [UNESP] Cilli, Eduardo M. [UNESP] Costa-Filho, Antonio J. |
author_role |
author |
author2 |
Vicente, Eduardo F. [UNESP] Crusca, Edson [UNESP] Cilli, Eduardo M. [UNESP] Costa-Filho, Antonio J. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade de São Paulo (USP) Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Basso, Luis G.M. Vicente, Eduardo F. [UNESP] Crusca, Edson [UNESP] Cilli, Eduardo M. [UNESP] Costa-Filho, Antonio J. |
description |
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. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-11-28 2018-12-11T17:08:03Z 2018-12-11T17:08:03Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1038/srep37131 Scientific Reports, v. 6. 2045-2322 http://hdl.handle.net/11449/173854 10.1038/srep37131 2-s2.0-84999663587 2-s2.0-84999663587.pdf |
url |
http://dx.doi.org/10.1038/srep37131 http://hdl.handle.net/11449/173854 |
identifier_str_mv |
Scientific Reports, v. 6. 2045-2322 10.1038/srep37131 2-s2.0-84999663587 2-s2.0-84999663587.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Scientific Reports 1,533 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
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1797789499678261248 |