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A fusion peptide in preS1 and the human protein disulfide isomerase ERp57 are involved in hepatitis B virus membrane fusion process

Cell entry of enveloped viruses relies on the fusion between the viral and plasma or endosomal membranes, through a mechanism that is triggered by a cellular signal. Here we used a combination of computational and experimental approaches to unravel the main determinants of hepatitis B virus (HBV) me...

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Autores principales: Pérez-Vargas, Jimena, Teppa, Elin, Amirache, Fouzia, Boson, Bertrand, Pereira de Oliveira, Rémi, Combet, Christophe, Böckmann, Anja, Fusil, Floriane, Freitas, Natalia, Carbone, Alessandra, Cosset, François-Loïc
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8282342/
https://www.ncbi.nlm.nih.gov/pubmed/34190687
http://dx.doi.org/10.7554/eLife.64507
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author Pérez-Vargas, Jimena
Teppa, Elin
Amirache, Fouzia
Boson, Bertrand
Pereira de Oliveira, Rémi
Combet, Christophe
Böckmann, Anja
Fusil, Floriane
Freitas, Natalia
Carbone, Alessandra
Cosset, François-Loïc
author_facet Pérez-Vargas, Jimena
Teppa, Elin
Amirache, Fouzia
Boson, Bertrand
Pereira de Oliveira, Rémi
Combet, Christophe
Böckmann, Anja
Fusil, Floriane
Freitas, Natalia
Carbone, Alessandra
Cosset, François-Loïc
author_sort Pérez-Vargas, Jimena
collection PubMed
description Cell entry of enveloped viruses relies on the fusion between the viral and plasma or endosomal membranes, through a mechanism that is triggered by a cellular signal. Here we used a combination of computational and experimental approaches to unravel the main determinants of hepatitis B virus (HBV) membrane fusion process. We discovered that ERp57 is a host factor critically involved in triggering HBV fusion and infection. Then, through modeling approaches, we uncovered a putative allosteric cross-strand disulfide (CSD) bond in the HBV S glycoprotein and we demonstrate that its stabilization could prevent membrane fusion. Finally, we identified and characterized a potential fusion peptide in the preS1 domain of the HBV L glycoprotein. These results underscore a membrane fusion mechanism that could be triggered by ERp57, allowing a thiol/disulfide exchange reaction to occur and regulate isomerization of a critical CSD, which ultimately leads to the exposition of the fusion peptide.
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spelling pubmed-82823422021-07-19 A fusion peptide in preS1 and the human protein disulfide isomerase ERp57 are involved in hepatitis B virus membrane fusion process Pérez-Vargas, Jimena Teppa, Elin Amirache, Fouzia Boson, Bertrand Pereira de Oliveira, Rémi Combet, Christophe Böckmann, Anja Fusil, Floriane Freitas, Natalia Carbone, Alessandra Cosset, François-Loïc eLife Computational and Systems Biology Cell entry of enveloped viruses relies on the fusion between the viral and plasma or endosomal membranes, through a mechanism that is triggered by a cellular signal. Here we used a combination of computational and experimental approaches to unravel the main determinants of hepatitis B virus (HBV) membrane fusion process. We discovered that ERp57 is a host factor critically involved in triggering HBV fusion and infection. Then, through modeling approaches, we uncovered a putative allosteric cross-strand disulfide (CSD) bond in the HBV S glycoprotein and we demonstrate that its stabilization could prevent membrane fusion. Finally, we identified and characterized a potential fusion peptide in the preS1 domain of the HBV L glycoprotein. These results underscore a membrane fusion mechanism that could be triggered by ERp57, allowing a thiol/disulfide exchange reaction to occur and regulate isomerization of a critical CSD, which ultimately leads to the exposition of the fusion peptide. eLife Sciences Publications, Ltd 2021-06-30 /pmc/articles/PMC8282342/ /pubmed/34190687 http://dx.doi.org/10.7554/eLife.64507 Text en © 2021, Pérez-Vargas et al https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Computational and Systems Biology
Pérez-Vargas, Jimena
Teppa, Elin
Amirache, Fouzia
Boson, Bertrand
Pereira de Oliveira, Rémi
Combet, Christophe
Böckmann, Anja
Fusil, Floriane
Freitas, Natalia
Carbone, Alessandra
Cosset, François-Loïc
A fusion peptide in preS1 and the human protein disulfide isomerase ERp57 are involved in hepatitis B virus membrane fusion process
title A fusion peptide in preS1 and the human protein disulfide isomerase ERp57 are involved in hepatitis B virus membrane fusion process
title_full A fusion peptide in preS1 and the human protein disulfide isomerase ERp57 are involved in hepatitis B virus membrane fusion process
title_fullStr A fusion peptide in preS1 and the human protein disulfide isomerase ERp57 are involved in hepatitis B virus membrane fusion process
title_full_unstemmed A fusion peptide in preS1 and the human protein disulfide isomerase ERp57 are involved in hepatitis B virus membrane fusion process
title_short A fusion peptide in preS1 and the human protein disulfide isomerase ERp57 are involved in hepatitis B virus membrane fusion process
title_sort fusion peptide in pres1 and the human protein disulfide isomerase erp57 are involved in hepatitis b virus membrane fusion process
topic Computational and Systems Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8282342/
https://www.ncbi.nlm.nih.gov/pubmed/34190687
http://dx.doi.org/10.7554/eLife.64507
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