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Related Concept Videos

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...
Viral Recombination00:57

Viral Recombination

Cells are sometimes infected by more than one virus at once. When two viruses disassemble to expose their genomes for replication in the same cell, similar regions of their genomes can pair together and exchange sequences in a process called recombination. Alternatively, viruses with segmented genomes can swap segments in a process called reassortment.
Subviral Agents01:29

Subviral Agents

Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
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: Jun 24, 2026

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

Generalized structural polymorphism in self-assembled viral particles.

Hung D Nguyen1, Charles L Brooks

  • 1Department of Chemistry, 930 North University Avenue, University of Michigan, Ann Arbor, Michigan 48109, USA.

Nano Letters
|April 16, 2009
PubMed
Summary
This summary is machine-generated.

Viral capsid self-assembly can lead to aberrant structures. Molecular dynamics simulations reveal inherent structural polymorphism in coat proteins, forming both larger and smaller aberrant capsules alongside icosahedral ones.

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Area of Science:

  • Structural biology
  • Computational biophysics
  • Virology

Background:

  • Nearly all spherical viruses possess protein shells (capsids) with icosahedral symmetry.
  • Viral capsid self-assembly can result in misassembled, aberrant structures.

Purpose of the Study:

  • To investigate the spontaneous self-assembly of viral capsids using molecular dynamics simulations.
  • To explore the structural polymorphism of viral capsids formed from pentameric and hexameric protein subunits.
  • To understand the kinetic mechanisms underlying the formation of aberrant viral capsids.

Main Methods:

  • Molecular dynamics simulations were employed to model the self-assembly of viral capsids.
  • Simulations utilized simple models of coat proteins preassembled into pentameric and hexameric capsomers.
  • Simulations covered capsid sizes ranging from T = 1 to T = 19.

Main Results:

  • Observed self-assembly into both icosahedral capsids and various non-icosahedral, ordered capsules.
  • Demonstrated that structural polymorphism is an intrinsic property of coat proteins, irrespective of capsid complexity.
  • Identified two classes of aberrant structures: larger capsules in T = 1-7 systems and smaller capsules in T = 7-19 systems.

Conclusions:

  • Coat protein structural polymorphism is inherent and influences capsid self-assembly outcomes.
  • Distinct kinetic mechanisms govern the formation of aberrant structures, offering insights into controlling icosahedral capsid assembly.
  • Understanding these mechanisms is crucial for deciphering viral assembly pathways and potentially designing novel viral nanoparticles.