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Phosphorylation of the Arginine-Rich C-Terminal Domains of the Hepatitis B Virus (HBV) Core Protein as a Fine Regulator of the Interaction between HBc and Nucleic Acid

Abstract : The morphogenesis of Hepatitis B Virus (HBV) viral particles is nucleated by the oligomerization of HBc protein molecules, resulting in the formation of an icosahedral capsid shell containing the replication-competent nucleoprotein complex made of the viral polymerase and the pre-genomic RNA (pgRNA). HBc is a phospho-protein containing two distinct domains acting together throughout the viral replication cycle. The N-terminal domain, (residues 1-140), shown to self-assemble, is linked by a short flexible domain to the basic C-terminal domain (residues 150-183) that interacts with nucleic acids (NAs). In addition, the C-terminal domain contains a series of phospho-acceptor residues that undergo partial phosphorylation and de-phosphorylation during virus replication. This highly dynamic process governs the homeostatic charge that is essential for capsid stability, pgRNA packaging and to expose the C-terminal domain at the surface of the particles for cell trafficking. In this review, we discuss the roles of the N-terminal and C-terminal domains of HBc protein during HBV morphogenesis, focusing on how the C-terminal domain phosphorylation dynamics regulate its interaction with nucleic acids throughout the assembly and maturation of HBV particles.
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https://www.hal.inserm.fr/inserm-02915282
Contributor : Hugues de Rocquigny <>
Submitted on : Friday, August 14, 2020 - 8:46:43 AM
Last modification on : Tuesday, August 18, 2020 - 3:28:20 AM
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Hugues de Rocquigny, Virgile Rat, Florentin Pastor, Jean-Luc Darlix, Christophe Hourioux, et al.. Phosphorylation of the Arginine-Rich C-Terminal Domains of the Hepatitis B Virus (HBV) Core Protein as a Fine Regulator of the Interaction between HBc and Nucleic Acid. Viruses, MDPI, 2020, 12 (7), pp.E738. ⟨10.3390/v12070738⟩. ⟨inserm-02915282⟩

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