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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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...
Protein Complex Assembly02:41

Protein Complex Assembly

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...
Viral Structure00:56

Viral Structure

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.
Size and Structure of Viral Genomes01:26

Size and Structure of Viral Genomes

Viral genomes exhibit remarkable diversity in size, structure, and composition, influencing their replication strategies and interactions with host cells. These genomes consist of either DNA or RNA and may be linear or circular. Additionally, they can be single-stranded or double-stranded, with each configuration affecting how the virus propagates within a host. RNA viruses, for instance, generally have smaller genomes than DNA viruses, a factor that contributes to their high mutation rates and...
Introduction to Virus01:28

Introduction to Virus

Viruses are unique biological entities that blur the boundary between living and non-living systems. Although they lack cellular structure and metabolic processes, they can exhibit characteristics of life when infecting a host. Their defining feature is a nucleic acid core, composed of either DNA or RNA, encapsulated within a protein coat called a capsid. This simple structure allows them to invade host cells and use their machinery for replication efficiently.Viral Structure and...
Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...

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Related Experiment Video

Updated: Jul 11, 2026

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
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Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction

Published on: August 9, 2011

Exploring the parameter space of complex self-assembly through virus capsid models.

Blake Sweeney1, Tiequan Zhang, Russell Schwartz

  • 1Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania, USA.

Biophysical Journal
|October 9, 2007
PubMed
Summary

Viral capsid assembly pathways vary significantly with binding rates. Modest changes in conditions can alter assembly mechanisms, highlighting caution needed when extrapolating in vitro or model findings to in vivo systems.

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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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Related Experiment Videos

Last Updated: Jul 11, 2026

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
12:38

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction

Published on: August 9, 2011

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly
09:47

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

Published on: March 1, 2012

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
09:08

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

Published on: July 27, 2021

Area of Science:

  • Biophysics
  • Computational Biology
  • Virology

Background:

  • Viral capsid assembly is crucial for virus replication and represents a complex self-assembly process.
  • Understanding the factors that govern capsid formation is essential for developing antiviral strategies.

Purpose of the Study:

  • To characterize the parameter space of icosahedral viral capsid assembly using discrete event stochastic simulations.
  • To identify distinct assembly mechanisms and unproductive regions within the parameter space.
  • To compare the assembly dynamics of an icosahedral system with a simpler octamer system.

Main Methods:

  • Discrete event stochastic simulations were employed to model icosahedral viral capsid assembly.
  • The simulations explored the parameter space as a function of monomer-monomer binding rates.
  • A simpler octamer system was simulated for comparative analysis.

Main Results:

  • Three major assembly mechanisms were identified: nucleation-limited monomer-accretion and two hierarchical pathways.
  • Unproductive regions containing kinetically trapped species were also observed.
  • The icosahedral model exhibited high sensitivity to parameter variations, unlike the less sensitive octamer model.
  • Modest changes in assembly conditions significantly shifted assembly pathways.

Conclusions:

  • Assembly pathways are highly sensitive to parameter variations, especially in complex icosahedral systems.
  • Differences between in vitro and in vivo assembly conditions can lead to substantial shifts in observed pathways.
  • Conclusions drawn from theoretical models or in vitro experiments regarding in vivo capsid assembly dynamics should be made with caution.