4.3 Review Book Chapter

The Structural Biology of Hepatitis B Virus: Form and Function

期刊

ANNUAL REVIEW OF VIROLOGY, VOL 3
卷 3, 期 -, 页码 429-451

出版社

ANNUAL REVIEWS
DOI: 10.1146/annurev-virology-110615-042238

关键词

antiviral; capsid; icosahedral; nucleoprotein complex; reverse transcriptase; self-assembly

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资金

  1. NIAID NIH HHS [R01 AI067417, R01 AI118933] Funding Source: Medline
  2. NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI118933, R01AI067417] Funding Source: NIH RePORTER

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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.

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