Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replication

E2, along with Erns and E1, is an envelope glycoprotein of Classical Swine Fever Virus (CSFV). E2 is involved in several virus functions: cell attachment, host range susceptibility and virulence in natural hosts. Here we evaluate the role of a specific E2 region, 818CPIGWTGVIEC828, containing a puta...

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Autores: Fernández Sainz, Ignacio, Largo Pereda, Eneko, Gladue, Douglas P., O’Donnell, Vivian, Holinka, Lauren G., Carey, L.B., Lu, X, Nieva Escandón, José Luis, Borca, Manuel V.
Tipo de recurso: artículo
Fecha de publicación:2014
País:España
Institución:Universidad del País Vasco
Repositorio:Addi. Archivo Digital para la Docencia y la Investigación
OAI Identifier:oai:addi.ehu.eus:10810/65556
Acceso en línea:http://hdl.handle.net/10810/65556
Access Level:acceso abierto
Palabra clave:fusion peptide
CSFV
pestivirus
classical swine fever virus
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spelling Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replicationFernández Sainz, IgnacioLargo Pereda, EnekoGladue, Douglas P.O’Donnell, VivianHolinka, Lauren G.Carey, L.B.Lu, XNieva Escandón, José LuisBorca, Manuel V.fusion peptideCSFVpestivirusclassical swine fever virusE2, along with Erns and E1, is an envelope glycoprotein of Classical Swine Fever Virus (CSFV). E2 is involved in several virus functions: cell attachment, host range susceptibility and virulence in natural hosts. Here we evaluate the role of a specific E2 region, 818CPIGWTGVIEC828, containing a putative fusion peptide (FP) sequence. Reverse genetics utilizing a full-length infectious clone of the highly virulent CSFV strain Brescia (BICv) was used to evaluate how individual amino acid substitutions within this region of E2 may affect replication of BICv. A synthetic peptide representing the complete E2 FP amino acid sequence adopted a β-type extended conformation in membrane mimetics, penetrated into model membranes, and perturbed lipid bilayer integrity in vitro. Similar peptides harboring amino acid substitutions adopted comparable conformations but exhibited different membrane activities. Therefore, a preliminary characterization of the putative FP 818CPIGWTGVIEC828 indicates a membrane fusion activity and a critical role in virus replication.This study was in part supported by Spanish MINECO and Basque Government grants (BIO2011-29792 and IT838-13 to J.L.N.). We thank the Plum Island Animal Disease Center animal care unit staff for excellent technical assistance. We specially thank Melanie Prarat for editing the manuscript.Elsevier202420242014info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10810/65556reponame:Addi. Archivo Digital para la Docencia y la Investigacióninstname:Universidad del País VascoIngléshttps://www.sciencedirect.com/science/article/pii/S0042682214000877info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/3.0/es/Atribución-NoComercial-SinDerivadas 3.0 Españaoai:addi.ehu.eus:10810/655562026-06-18T09:23:17Z
dc.title.none.fl_str_mv Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replication
title Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replication
spellingShingle Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replication
Fernández Sainz, Ignacio
fusion peptide
CSFV
pestivirus
classical swine fever virus
title_short Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replication
title_full Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replication
title_fullStr Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replication
title_full_unstemmed Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replication
title_sort Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replication
dc.creator.none.fl_str_mv Fernández Sainz, Ignacio
Largo Pereda, Eneko
Gladue, Douglas P.
O’Donnell, Vivian
Holinka, Lauren G.
Carey, L.B.
Lu, X
Nieva Escandón, José Luis
Borca, Manuel V.
author Fernández Sainz, Ignacio
author_facet Fernández Sainz, Ignacio
Largo Pereda, Eneko
Gladue, Douglas P.
O’Donnell, Vivian
Holinka, Lauren G.
Carey, L.B.
Lu, X
Nieva Escandón, José Luis
Borca, Manuel V.
author_role author
author2 Largo Pereda, Eneko
Gladue, Douglas P.
O’Donnell, Vivian
Holinka, Lauren G.
Carey, L.B.
Lu, X
Nieva Escandón, José Luis
Borca, Manuel V.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv fusion peptide
CSFV
pestivirus
classical swine fever virus
topic fusion peptide
CSFV
pestivirus
classical swine fever virus
description E2, along with Erns and E1, is an envelope glycoprotein of Classical Swine Fever Virus (CSFV). E2 is involved in several virus functions: cell attachment, host range susceptibility and virulence in natural hosts. Here we evaluate the role of a specific E2 region, 818CPIGWTGVIEC828, containing a putative fusion peptide (FP) sequence. Reverse genetics utilizing a full-length infectious clone of the highly virulent CSFV strain Brescia (BICv) was used to evaluate how individual amino acid substitutions within this region of E2 may affect replication of BICv. A synthetic peptide representing the complete E2 FP amino acid sequence adopted a β-type extended conformation in membrane mimetics, penetrated into model membranes, and perturbed lipid bilayer integrity in vitro. Similar peptides harboring amino acid substitutions adopted comparable conformations but exhibited different membrane activities. Therefore, a preliminary characterization of the putative FP 818CPIGWTGVIEC828 indicates a membrane fusion activity and a critical role in virus replication.
publishDate 2014
dc.date.none.fl_str_mv 2014
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10810/65556
url http://hdl.handle.net/10810/65556
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://www.sciencedirect.com/science/article/pii/S0042682214000877
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/3.0/es/
Atribución-NoComercial-SinDerivadas 3.0 España
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/3.0/es/
Atribución-NoComercial-SinDerivadas 3.0 España
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Addi. Archivo Digital para la Docencia y la Investigación
instname:Universidad del País Vasco
instname_str Universidad del País Vasco
reponame_str Addi. Archivo Digital para la Docencia y la Investigación
collection Addi. Archivo Digital para la Docencia y la Investigación
repository.name.fl_str_mv
repository.mail.fl_str_mv
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