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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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2021
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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. |
format | Online Article Text |
id | pubmed-8282342 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
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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