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Related Concept Videos

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...
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.
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...
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...
Retrovirus Life Cycles01:10

Retrovirus Life Cycles

Retroviruses have a single-stranded RNA genome that undergoes a special form of replication. Once the retrovirus has entered the host cell, an enzyme called reverse transcriptase synthesizes double-stranded DNA from the retroviral RNA genome. This DNA copy of the genome is then integrated into the host’s genome inside the nucleus via an enzyme called integrase. Consequently, the retroviral genome is transcribed into RNA whenever the host’s genome is transcribed, allowing the retrovirus to...
What are Viruses?00:50

What are Viruses?

Overview

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Related Experiment Video

Updated: Jul 19, 2026

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

Irreversible growth model for virus capsid assembly.

Stephen D Hicks1, C L Henley

  • 1Department of Physics, Cornell University, Ithaca, New York 14853, USA. sdh33@cornell.edu

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|October 10, 2006
PubMed
Summary

This study models virus capsid assembly using irreversible steps and local information, generating irregular capsid structures. Capsid size and shape are influenced by elastic properties and spontaneous curvature, offering insights into retroviral capsid formation.

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In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
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In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation

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Related Experiment Videos

Last Updated: Jul 19, 2026

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

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

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
07:24

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation

Published on: March 27, 2016

Area of Science:

  • Biophysics
  • Computational Biology
  • Structural Biology

Background:

  • Virus capsid assembly is crucial for viral replication and pathogenesis.
  • Many viruses, like retroviruses (e.g., HIV), exhibit irregular capsid structures, contrasting with well-studied icosahedral viruses.
  • Understanding the principles governing spontaneous capsid formation is key to developing antiviral strategies.

Purpose of the Study:

  • To model the spontaneous assembly of virus capsids from identical subunits.
  • To investigate the influence of elastic properties and local information on capsid formation.
  • To explore the generation of irregular capsid structures relevant to retroviruses.

Main Methods:

  • Formulation of an elastic Hamiltonian including stretching, bending stiffness, and spontaneous curvature.
  • Incorporation of rate constants for subunit addition and bond formation.
  • Simulation of capsid assembly using irreversible steps and local growth information.

Main Results:

  • Generated an ensemble of irregular capsid structures, distinct from icosahedral symmetry.
  • Observed an exponential decay in successful capsid completion probability with increasing size.
  • Determined that capsid size is strongly dependent on spontaneous curvature and weakly on elastic stiffness ratios.
  • Found that the facetedness (localization of Gaussian curvature) is highly sensitive to the ratio of bending to stretching stiffness.

Conclusions:

  • The developed model plausibly explains the formation of irregular capsids found in retroviruses.
  • Spontaneous curvature and elastic properties are critical determinants of capsid size and morphology.
  • The findings provide a framework for understanding the biophysics of non-icosahedral viral capsid assembly.