Conformational plasticity underlies membrane fusion induced by an HIV sequence juxtaposed to the lipid envelope

Abstract 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 exter...

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Autores principales:	Igor de la Arada, Johana Torralba, Igor Tascón, Adai Colom, Iban Ubarretxena-Belandia, José L. R. Arrondo, Beatriz Apellániz, José L. Nieva
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a3e2efe9aa6549b1a75f84485d650250
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spelling	oai:doaj.org-article:a3e2efe9aa6549b1a75f84485d6502502021-12-02T15:23:09ZConformational plasticity underlies membrane fusion induced by an HIV sequence juxtaposed to the lipid envelope10.1038/s41598-020-80156-w2045-2322https://doaj.org/article/a3e2efe9aa6549b1a75f84485d6502502021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-80156-whttps://doaj.org/toc/2045-2322Abstract 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.Igor de la AradaJohana TorralbaIgor TascónAdai ColomIban Ubarretxena-BelandiaJosé L. R. ArrondoBeatriz ApellánizJosé L. NievaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Igor de la Arada Johana Torralba Igor Tascón Adai Colom Iban Ubarretxena-Belandia José L. R. Arrondo Beatriz Apellániz José L. Nieva Conformational plasticity underlies membrane fusion induced by an HIV sequence juxtaposed to the lipid envelope
description	Abstract 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.
format	article
author	Igor de la Arada Johana Torralba Igor Tascón Adai Colom Iban Ubarretxena-Belandia José L. R. Arrondo Beatriz Apellániz José L. Nieva
author_facet	Igor de la Arada Johana Torralba Igor Tascón Adai Colom Iban Ubarretxena-Belandia José L. R. Arrondo Beatriz Apellániz José L. Nieva
author_sort	Igor de la Arada
title	Conformational plasticity underlies membrane fusion induced by an HIV sequence juxtaposed to the lipid envelope
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
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/a3e2efe9aa6549b1a75f84485d650250
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Conformational plasticity underlies membrane fusion induced by an HIV sequence juxtaposed to the lipid envelope

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