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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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Viral Structure00:56

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Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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The Nucleosome Core Particle01:12

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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Intracellular Movement of Viruses and Bacteria01:10

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Intracellular bacteria and viruses often comprise a group of highly infectious pathogens that can cause several diseases. Bacterial pathogens include those belonging to the genus Rickettsia responsible for conditions such as rocky mountain spotted fever and the Mediterranean spotted fever; Chlamydia, a genus responsible for a sexually transmitted disease; Coxiella burnetii, an agent responsible for Q fever. Viral pathogens include vaccinia—a poxvirus, and herpes simplex virus—a...
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Related Experiment Video

Updated: May 17, 2025

Development of a Hepatitis B Virus Reporter System to Monitor the Early Stages of the Replication Cycle
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Development of a Hepatitis B Virus Reporter System to Monitor the Early Stages of the Replication Cycle

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Hepatitis B Virus Nucleocapsid Assembly.

Xupeng Hong1, William M Schneider1, Charles M Rice1

  • 1Laboratory of Virology and Infectious Disease, The Rockefeller University, New York, NY, USA.

Journal of Molecular Biology
|May 2, 2025
PubMed
Summary
This summary is machine-generated.

Hepatitis B virus (HBV) nucleocapsid assembly involves packaging viral RNA and polymerase into capsids. New cell-free systems are needed to fully understand and target this process for chronic hepatitis B cures.

Keywords:
genome packaginghepatitis B virushost factornucleocapsid assemblyviral polymerase

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Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly
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Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly

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Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
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Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

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Related Experiment Videos

Last Updated: May 17, 2025

Development of a Hepatitis B Virus Reporter System to Monitor the Early Stages of the Replication Cycle
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Development of a Hepatitis B Virus Reporter System to Monitor the Early Stages of the Replication Cycle

Published on: February 1, 2017

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Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly
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Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly

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Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
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Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

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Area of Science:

  • Virology
  • Molecular Biology
  • Hepatology

Background:

  • Hepatitis B virus (HBV) replicates its DNA genome via reverse transcription of a pregenomic RNA (pgRNA) precursor.
  • Nucleocapsid assembly, the selective packaging of pgRNA and viral polymerase (Pol) into capsids, is critical for HBV lifecycle.
  • Current understanding relies on cellular and cell-free systems, but a complete reconstitution system is lacking.

Purpose of the Study:

  • To review current knowledge on HBV nucleocapsid assembly.
  • To highlight the interplay between Pol-pgRNA interactions, capsid formation, and host factors.
  • To underscore the need for novel systems to reconstitute complete HBV nucleocapsid assembly.

Main Methods:

  • Review of existing literature on HBV nucleocapsid assembly.
  • Analysis of insights gained from cellular and cell-free systems.
  • Discussion of therapeutic strategies targeting nucleocapsid assembly.

Main Results:

  • Significant insights into capsid assembly, Pol-pgRNA binding, and replication initiation have been achieved.
  • The absence of a complete cell-free system for selective HBV Pol-pgRNA packaging remains a key limitation.
  • Host factors play a regulatory role in HBV nucleocapsid assembly.

Conclusions:

  • Targeting Pol-pgRNA interactions and nucleocapsid assembly is a promising therapeutic strategy for chronic hepatitis B.
  • Developing inhibitors of nucleocapsid assembly, some in clinical trials, offers a potential cure for chronic HBV.
  • Further research using advanced systems is crucial to fully elucidate HBV nucleocapsid assembly mechanisms.