dc.contributor.author | De la Arada Echevarría, Igor ![ORCID](/themes/Mirage2//images/orcid_16x16.png) | |
dc.contributor.author | Torralba Iturbe, Johana ![ORCID](/themes/Mirage2//images/orcid_16x16.png) | |
dc.contributor.author | Tascón, Igor | |
dc.contributor.author | Colom Diego, Adai | |
dc.contributor.author | Ubarrechena Belandia, Iván ![ORCID](/themes/Mirage2//images/orcid_16x16.png) | |
dc.contributor.author | Rodríguez Arrondo, José Luis | |
dc.contributor.author | Apellaniz Unzalu, Beatriz ![ORCID](/themes/Mirage2//images/orcid_16x16.png) | |
dc.contributor.author | Nieva Escandón, José Luis | |
dc.date.accessioned | 2021-03-11T11:14:20Z | |
dc.date.available | 2021-03-11T11:14:20Z | |
dc.date.issued | 2021-01-14 | |
dc.identifier.citation | Scientific Reports 11(1) : (2021) // Article ID 1278 | es_ES |
dc.identifier.issn | 2045-2322 | |
dc.identifier.uri | http://hdl.handle.net/10810/50573 | |
dc.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 | es_ES |
dc.description.sponsorship | This 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 acknowledged | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Springer Nature | es_ES |
dc.relation | info:eu-repo/grantAgreement/MICINN/RTI2018-095624-B-C21 | es_ES |
dc.relation | info:eu-repo/grantAgreement/MICINN/PID2019-111096GA-I00 | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | * |
dc.subject | envelope glycoproteins | es_ES |
dc.subject | fusion peptides | es_ES |
dc.subject | target cells | es_ES |
dc.subject | aromatic residues | es_ES |
dc.subject | viral fusion glycoproteins | es_ES |
dc.subject | infrared spectroscopy | es_ES |
dc.subject | cryo-electron microscopy | es_ES |
dc.subject | cholesterol | es_ES |
dc.title | Conformational Plasticity Underlies Membrane Fusion Induced by an HIV Sequence Juxtaposed to the Lipid Envelope | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.rights.holder | This article is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0) | es_ES |
dc.rights.holder | Atribución 3.0 España | * |
dc.relation.publisherversion | https://www.nature.com/articles/s41598-020-80156-w | es_ES |
dc.identifier.doi | 10.1038/s41598-020-80156-w | |
dc.departamentoes | Bioquímica y biología molecular | es_ES |
dc.departamentoes | Fisiología | es_ES |
dc.departamentoeu | Biokimika eta biologia molekularra | es_ES |
dc.departamentoeu | Fisiologia | es_ES |