Conformational Plasticity Underlies Membrane Fusion Induced by an HIV Sequence Juxtaposed to the Lipid Envelope

Envelope glycoproteins from genetically-divergent virus families comprise fusion peptides (FPs) that have been posited to insert and perturb the membranes of target cells upon activation of the virus-cell fusion reaction. Conserved sequences rich in aromatic residues juxtaposed to the external leafl...

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Autores: De la Arada Echevarría, Igor, Torralba Iturbe, Johana, Tascón, Igor, Colom Diego, Adai, Ubarrechena Belandia, Iván, Rodríguez Arrondo, José Luis, Apellaniz Unzalu, Beatriz, Nieva Escandón, José Luis
Tipo de recurso: artículo
Fecha de publicación:2021
País:España
Institución:Universidad del País Vasco
Repositorio:Addi. Archivo Digital para la Docencia y la Investigación
OAI Identifier:oai:addi.ehu.eus:10810/50573
Acceso en línea:http://hdl.handle.net/10810/50573
Access Level:acceso abierto
Palabra clave:envelope glycoproteins
fusion peptides
target cells
aromatic residues
viral fusion glycoproteins
infrared spectroscopy
cryo-electron microscopy
cholesterol
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spelling Conformational Plasticity Underlies Membrane Fusion Induced by an HIV Sequence Juxtaposed to the Lipid EnvelopeDe la Arada Echevarría, IgorTorralba Iturbe, JohanaTascón, IgorColom Diego, AdaiUbarrechena Belandia, IvánRodríguez Arrondo, José LuisApellaniz Unzalu, BeatrizNieva Escandón, José Luisenvelope glycoproteinsfusion peptidestarget cellsaromatic residuesviral fusion glycoproteinsinfrared spectroscopycryo-electron microscopycholesterolEnvelope glycoproteins from genetically-divergent virus families comprise fusion peptides (FPs) that have been posited to insert and perturb the membranes of target cells upon activation of the virus-cell fusion reaction. Conserved sequences rich in aromatic residues juxtaposed to the external leaflet of the virion-wrapping membranes are also frequently found in viral fusion glycoproteins. These membrane-proximal external regions (MPERs) have been implicated in the promotion of the viral membrane restructuring event required for fusion to proceed, hence, proposed to comprise supplementary FPs. However, it remains unknown whether the structure-function relationships governing canonical FPs also operate in the mirroring MPER sequences. Here, we combine infrared spectroscopy-based approaches with cryo-electron microscopy to analyze the alternating conformations adopted, and perturbations generated in membranes by CpreTM, a peptide derived from the MPER of the HIV-1 Env glycoprotein. Altogether, our structural and morphological data support a cholesterol-dependent conformational plasticity for this HIV-1 sequence, which could assist cell-virus fusion by destabilizing the viral membrane at the initial stages of the processThis study was supported by the Spanish MCIU (Grants RTI2018-095624-B-C21; MCIU/AEI/FEDER, UE to JLN and BA; and PID2019-111096GA-I00; MCIU/AEI/FEDER, UE to AC) and Basque Government (Grant: IT1196-19). Technical assistance from MI Collado and M Carril with 31P-NMR measurements and data processing is greatly acknowledgedSpringer Nature202120212021info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10810/50573reponame:Addi. Archivo Digital para la Docencia y la Investigacióninstname:Universidad del País VascoInglésinfo:eu-repo/grantAgreement/MICINN/RTI2018-095624-B-C21/info:eu-repo/grantAgreement/MICINN/PID2019-111096GA-I00/https://www.nature.com/articles/s41598-020-80156-winfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/3.0/es/This article is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0)Atribución 3.0 Españaoai:addi.ehu.eus:10810/505732026-06-18T09:23:17Z
dc.title.none.fl_str_mv Conformational Plasticity Underlies Membrane Fusion Induced by an HIV Sequence Juxtaposed to the Lipid Envelope
title Conformational Plasticity Underlies Membrane Fusion Induced by an HIV Sequence Juxtaposed to the Lipid Envelope
spellingShingle Conformational Plasticity Underlies Membrane Fusion Induced by an HIV Sequence Juxtaposed to the Lipid Envelope
De la Arada Echevarría, Igor
envelope glycoproteins
fusion peptides
target cells
aromatic residues
viral fusion glycoproteins
infrared spectroscopy
cryo-electron microscopy
cholesterol
title_short Conformational Plasticity Underlies Membrane Fusion Induced by an HIV Sequence Juxtaposed to the Lipid Envelope
title_full Conformational Plasticity Underlies Membrane Fusion Induced by an HIV Sequence Juxtaposed to the Lipid Envelope
title_fullStr Conformational Plasticity Underlies Membrane Fusion Induced by an HIV Sequence Juxtaposed to the Lipid Envelope
title_full_unstemmed Conformational Plasticity Underlies Membrane Fusion Induced by an HIV Sequence Juxtaposed to the Lipid Envelope
title_sort Conformational Plasticity Underlies Membrane Fusion Induced by an HIV Sequence Juxtaposed to the Lipid Envelope
dc.creator.none.fl_str_mv De la Arada Echevarría, Igor
Torralba Iturbe, Johana
Tascón, Igor
Colom Diego, Adai
Ubarrechena Belandia, Iván
Rodríguez Arrondo, José Luis
Apellaniz Unzalu, Beatriz
Nieva Escandón, José Luis
author De la Arada Echevarría, Igor
author_facet De la Arada Echevarría, Igor
Torralba Iturbe, Johana
Tascón, Igor
Colom Diego, Adai
Ubarrechena Belandia, Iván
Rodríguez Arrondo, José Luis
Apellaniz Unzalu, Beatriz
Nieva Escandón, José Luis
author_role author
author2 Torralba Iturbe, Johana
Tascón, Igor
Colom Diego, Adai
Ubarrechena Belandia, Iván
Rodríguez Arrondo, José Luis
Apellaniz Unzalu, Beatriz
Nieva Escandón, José Luis
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv envelope glycoproteins
fusion peptides
target cells
aromatic residues
viral fusion glycoproteins
infrared spectroscopy
cryo-electron microscopy
cholesterol
topic envelope glycoproteins
fusion peptides
target cells
aromatic residues
viral fusion glycoproteins
infrared spectroscopy
cryo-electron microscopy
cholesterol
description Envelope glycoproteins from genetically-divergent virus families comprise fusion peptides (FPs) that have been posited to insert and perturb the membranes of target cells upon activation of the virus-cell fusion reaction. Conserved sequences rich in aromatic residues juxtaposed to the external leaflet of the virion-wrapping membranes are also frequently found in viral fusion glycoproteins. These membrane-proximal external regions (MPERs) have been implicated in the promotion of the viral membrane restructuring event required for fusion to proceed, hence, proposed to comprise supplementary FPs. However, it remains unknown whether the structure-function relationships governing canonical FPs also operate in the mirroring MPER sequences. Here, we combine infrared spectroscopy-based approaches with cryo-electron microscopy to analyze the alternating conformations adopted, and perturbations generated in membranes by CpreTM, a peptide derived from the MPER of the HIV-1 Env glycoprotein. Altogether, our structural and morphological data support a cholesterol-dependent conformational plasticity for this HIV-1 sequence, which could assist cell-virus fusion by destabilizing the viral membrane at the initial stages of the process
publishDate 2021
dc.date.none.fl_str_mv 2021
2021
2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10810/50573
url http://hdl.handle.net/10810/50573
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/grantAgreement/MICINN/RTI2018-095624-B-C21/
info:eu-repo/grantAgreement/MICINN/PID2019-111096GA-I00/
https://www.nature.com/articles/s41598-020-80156-w
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/3.0/es/
This article is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0)
Atribución 3.0 España
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/3.0/es/
This article is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0)
Atribución 3.0 España
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Springer Nature
publisher.none.fl_str_mv Springer Nature
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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score 15,300719

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