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A fusion peptide in preS1 and the human protein-disulfide isomerase ERp57 are involved in HBV membrane fusion process

Abstract : 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 modelling 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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https://hal.sorbonne-universite.fr/hal-03275938
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Submitted on : Thursday, July 1, 2021 - 3:03:16 PM
Last modification on : Thursday, September 2, 2021 - 9:08:50 AM

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Jimena Pérez-Vargas, Elin Teppa, Fouzia Amirache, Bertrand Boson, Rémi Pereira de Oliveira, et al.. A fusion peptide in preS1 and the human protein-disulfide isomerase ERp57 are involved in HBV membrane fusion process. eLife, eLife Sciences Publication, 2021, 10, ⟨10.7554/eLife.64507⟩. ⟨hal-03275938⟩

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