| Literature DB >> 27482896 |
Balasubramanian Venkatakrishnan1, Adam Zlotnick1.
Abstract
Hepatitis B virus is one of the smallest human pathogens, encoded by a 3,200-bp genome with only four open reading frames. Yet the virus shows a remarkable diversity in structural features, often with the same proteins adopting several conformations. In part, this is the parsimony of viruses, where a minimal number of proteins perform a wide variety of functions. However, a more important theme is that weak interactions between components as well as components with multiple conformations that have similar stabilities lead to a highly dynamic system. In hepatitis B virus, this is manifested as a virion where the envelope proteins have multiple structures, the envelope-capsid interaction is irregular, and the capsid is a dynamic compartment that actively participates in metabolism of the encapsidated genome and carries regulated signals for intracellular trafficking.Entities:
Keywords: antiviral; capsid; icosahedral; nucleoprotein complex; reverse transcriptase; self-assembly
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Year: 2016 PMID: 27482896 PMCID: PMC5646271 DOI: 10.1146/annurev-virology-110615-042238
Source DB: PubMed Journal: Annu Rev Virol ISSN: 2327-056X Impact factor: 10.431