The Hepatitis B virus large envelope protein initiates virion assembly by recruiting pre-assembled capsids at membrane rich domains related to late endosome

Author:

Seigneuret Florian1,Eymieux Sébastien1,Sarabia-Vega Vanessa1,Lemoine Roxane1,Burlaud-Gaillard Julien1,Raynal Pierre1,Hourioux Christophe1,Sureau Camille1,Roingeard Philippe2,de Rocquigny Hugues2ORCID

Affiliation:

1. Université de Tours Faculté de Médecine: Universite de Tours Faculte de Medecine

2. Universite de Tours Faculte de Medecine

Abstract

Abstract

A crucial step of HBV (Hepatitis B Virus) virion morphogenesis is the envelopment of the nucleocapsid by the viral envelope proteins, which is triggered by an interaction between the HBV core protein and the large HBV envelope protein. To document this interaction, we co-expressed core and large HBV envelope (LHBs) in Huh-7 cells and subjected the cells to microscopy examination by Fluorescence Resonance Energy Transfer (FRET) and Transmission Electron Microscopy (TEM). Our results show that the sole expression of the core protein leads to assembly of capsids that remain individually isolated within the whole cell, but particularly within the nucleus. In the presence of LHBs, capsids were observed as large clusters in a membrane rich region peripheral to the nucleus. In this context, core-LHBs complex co-localize with markers of the late endosome/multivesicular bodies, this co-localization being driven by LHBs. These results thus show that LHBs binds to the core proteins when preassembled into capsid, at membranes of the late endosome, where the inner capsid and the outer envelope meet to assemble a virion.

Publisher

Springer Science and Business Media LLC

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