The three lives of viral fusion peptides

Fusion peptides comprise conserved hydrophobic domains absolutely required for the fusogenic activity of glycoproteins from divergent virus families. After 30 years of intensive research efforts, the structures and functions underlying their high degree of sequence conservation are not fully elucida...

Descripción completa

Detalles Bibliográficos
Autores: Apellaniz Unzalu, Beatriz, Huarte Arrayago, Nerea, Largo Pereda, Eneko, Nieva Escandón, José Luis
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:10810/65548
Acceso en línea:http://hdl.handle.net/10810/65548
Access Level:acceso abierto
Palabra clave:fusion peptide
membrane fusion
viral entry
peptide-lipid interaction
id ES_2e60dff3394bc680cf8aba3d32b8762d
oai_identifier_str oai:addi.ehu.eus:10810/65548
network_acronym_str ES
network_name_str España
repository_id_str
spelling The three lives of viral fusion peptidesApellaniz Unzalu, BeatrizHuarte Arrayago, NereaLargo Pereda, EnekoNieva Escandón, José Luisfusion peptidemembrane fusionviral entrypeptide-lipid interactionFusion peptides comprise conserved hydrophobic domains absolutely required for the fusogenic activity of glycoproteins from divergent virus families. After 30 years of intensive research efforts, the structures and functions underlying their high degree of sequence conservation are not fully elucidated. The long-hydrophobic viral fusion peptide (VFP) sequences are structurally constrained to access three successive states after biogenesis. Firstly, the VFP sequence must fulfill the set of native interactions required for (meta) stable folding within the globular ectodomains of glycoprotein complexes. Secondly, at the onset of the fusion process, they get transferred into the target cell membrane and adopt specific conformations therein. According to commonly accepted mechanistic models, membrane-bound states of the VFP might promote the lipid bilayer remodeling required for virus-cell membrane merger. Finally, at least in some instances, several VFPs co-assemble with transmembrane anchors into membrane integral helical bundles, following a locking movement hypothetically coupled to fusion-pore expansion. Here we review different aspects of the three major states of the VFPs, including the functional assistance by other membrane-transferring glycoprotein regions, and discuss briefly their potential as targets for clinical intervention.We thank current financial support by the Spanish MINECO (BIO2011-29792), the Basque Government (IT838-13) and the National Institutes of Health (USA) (1R01AI097051-01). The authors acknowledge the contribution to their present understanding of VFP structure–function of many works not cited in this review due to space limitations.Elsevier202420242014info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10810/65548reponame:Addi. Archivo Digital para la Docencia y la Investigacióninstname:Universidad del País VascoInglésinfo:eu-repo/grantAgreement/MICIU/BIO2011-29792/https://www.sciencedirect.com/science/article/pii/S0009308414000413info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/3.0/es/© 2014 Elsevier. This manuscript version is made available under the CC-BY-NC-ND 4.0 license https://creativecommons.org/licenses/by-nc-nd/4.0/oai:addi.ehu.eus:10810/655482026-06-18T09:23:17Z
dc.title.none.fl_str_mv The three lives of viral fusion peptides
title The three lives of viral fusion peptides
spellingShingle The three lives of viral fusion peptides
Apellaniz Unzalu, Beatriz
fusion peptide
membrane fusion
viral entry
peptide-lipid interaction
title_short The three lives of viral fusion peptides
title_full The three lives of viral fusion peptides
title_fullStr The three lives of viral fusion peptides
title_full_unstemmed The three lives of viral fusion peptides
title_sort The three lives of viral fusion peptides
dc.creator.none.fl_str_mv Apellaniz Unzalu, Beatriz
Huarte Arrayago, Nerea
Largo Pereda, Eneko
Nieva Escandón, José Luis
author Apellaniz Unzalu, Beatriz
author_facet Apellaniz Unzalu, Beatriz
Huarte Arrayago, Nerea
Largo Pereda, Eneko
Nieva Escandón, José Luis
author_role author
author2 Huarte Arrayago, Nerea
Largo Pereda, Eneko
Nieva Escandón, José Luis
author2_role author
author
author
dc.subject.none.fl_str_mv fusion peptide
membrane fusion
viral entry
peptide-lipid interaction
topic fusion peptide
membrane fusion
viral entry
peptide-lipid interaction
description Fusion peptides comprise conserved hydrophobic domains absolutely required for the fusogenic activity of glycoproteins from divergent virus families. After 30 years of intensive research efforts, the structures and functions underlying their high degree of sequence conservation are not fully elucidated. The long-hydrophobic viral fusion peptide (VFP) sequences are structurally constrained to access three successive states after biogenesis. Firstly, the VFP sequence must fulfill the set of native interactions required for (meta) stable folding within the globular ectodomains of glycoprotein complexes. Secondly, at the onset of the fusion process, they get transferred into the target cell membrane and adopt specific conformations therein. According to commonly accepted mechanistic models, membrane-bound states of the VFP might promote the lipid bilayer remodeling required for virus-cell membrane merger. Finally, at least in some instances, several VFPs co-assemble with transmembrane anchors into membrane integral helical bundles, following a locking movement hypothetically coupled to fusion-pore expansion. Here we review different aspects of the three major states of the VFPs, including the functional assistance by other membrane-transferring glycoprotein regions, and discuss briefly their potential as targets for clinical intervention.
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/10810/65548
url http://hdl.handle.net/10810/65548
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/grantAgreement/MICIU/BIO2011-29792/
https://www.sciencedirect.com/science/article/pii/S0009308414000413
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/3.0/es/
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/3.0/es/
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
_version_ 1869405400533565440
score 15.300719

Similares en LA Referencia