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Seitz, S.* ; Habjanic, J. ; Schütz, A.K. ; Bartenschlager, R.*

The hepatitis B virus envelope proteins: Molecular gymnastics throughout the viral life cycle.

Annu. Rev. Virol. 7, 263-288 (2020)
DOI PMC
New hepatitis B virions released from infected hepatocytes are the result of an intricate maturation process that starts with the formation of the nucleocapsid providing a confined space where the viral DNA genome is synthesized via reverse transcription. Virion assembly is finalized by the enclosure of the icosahedral nucleocapsid within a heterogeneous envelope. The latter contains integral membrane proteins of three sizes, collectively known as hepatitis B surface antigen, and adopts multiple conformations in the course of the viral life cycle. The nucleocapsid conformation depends on the reverse transcription status of the genome, which in turn controls nucleocapsid interaction with the envelope proteins for virus exit. In addition, after secretion the virions undergo a distinct maturation step during which a topological switch of the large envelope protein confers infectivity. Here we review molecular determinants for envelopment and models that postulate molecular signals encoded in the capsid scaffold conducive or adverse to the recruitment of envelope proteins.
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Publication type Article: Journal article
Document type Review
Corresponding Author
Keywords Dane Particle ; Electron Microscopy ; Glycosylation ; Maturation Signal ; Membrane Protein ; Nucleocapsid ; Post-translational Modification ; Topological Switch ; Virion Maturation; Large Surface Protein; Amino-acid-sequence; Pre-s Domain; Immature Secretion Phenotype; Naturally-occurring Mutation; Precore Protein; Dane Particles; Core Protein; Transmembrane Topology; Dual Topology
ISSN (print) / ISBN 2327-056X
e-ISSN 2327-0578
Journal Annual review of virology
Quellenangaben Volume: 7, Issue: 1, Pages: 263-288 Article Number: , Supplement: ,
Publisher Annual Reviews
Publishing Place Palo Alto, California
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
Grants DFG, German Research Foundation
Deutsche Forschungsgemeinschaft (DFG, German Research foundation)