Capsid Assembly
Capsid Assembly - Related Videos
12:38
Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
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Cited by 8 •
2011
This article describes a method to obtain a three-dimensional (3D) structure of helically assembled molecules using cryo-electron microscopy. In this protocol, we use HIV-1 capsid assemblies to illustrate the detailed 3D reconstruction procedure for achieving a density map by the iterative helical real-space reconstruction method.
12:57
Alternative In Vitro Methods for the Determination of Viral Capsid Structural Integrity
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Cited by 6 •
2017
Routine detection methods utilizing viral genome amplification are limited by their inability to discriminate infectious from non-infectious particles. The purpose of this article is to provide detailed protocols for alternative methods to aid in discrimination of infectious norovirus particles using aptamer binding, dynamic light scattering, and transmission electron microscopy.
03:24
Visualizing Heat-Treated Viral Capsids Using Transmission Electron Microscopy
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2026
Source: Moore, M. D., et al. Alternative In Vitro Methods for the Determination of Viral Capsid Structural Integrity. J. Vis. Exp.(2017).This video demonstrates how purified viral capsids are heat-treated, prepared, and imaged using transmission electron microscopy (TEM) to reveal structural changes and heat-induced damage.
07:24
In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
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Cited by 4 •
2016
Disassembly of influenza A virus cores during virus entry into host cells is a multistep process. We describe an in vitro method to analyze the early stages of viral uncoating. In this approach, velocity gradient centrifugation is used to biochemically dissect the steps that initiate uncoating under defined conditions.
13:36
Utilizing the Antigen Capsid-Incorporation Strategy for the Development of Adenovirus Serotype 5-Vectored Vaccine Approaches
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Cited by 1 •
2015
Here, we present a protocol to generate a proof-of-principle divalent adenovirus type 5 (Ad5) vector Ad5/H5-HVR1-KWAS-HVR5-His6 by utilizing the Antigen Capsid-Incorporation strategy. This vector was demonstrated to exhibit qualitative fitness, the capability to escape Ad5-positive sera in vitro, and the antigenicity as well as immunogenicity to the incorporated antigens.
FAQs
Successful Capsid Assembly depends on coordinated contacts among structural proteins and, in some cases, between those proteins and the viral genome. These interactions help determine the order in which subunits associate and can promote conformational changes as the shell develops. Examining both interaction types helps explain how a particle acquires an organized structure rather than forming through random protein accumulation.
In some viruses, scaffold proteins guide the formation of the capsid before maturation. Their presence indicates that shell construction can involve temporary organizational factors, not only the structural proteins retained in the finished particle. Studying this stage helps distinguish assembly from maturation and clarifies how an initially formed shell can undergo later structural processing.
Conformational changes allow capsid components to adopt different structural states as assembly proceeds. These transitions can connect early subunit association with the formation of a mature particle that protects and stabilizes the genome. Because particle stability and infectivity are linked to successful maturation, identifying these changes helps explain how structural rearrangements influence viral function.
A focused study should consider the sequence of subunit association, the contacts between structural proteins, interactions with the viral genome, and any scaffold-guided stage that precedes maturation. Together, these features provide a framework for relating molecular events to shell organization, genome stabilization, particle stability, and infectivity without treating assembly as a single isolated step.
Capsid Assembly offers potential antiviral targets because disrupting its protein-protein interactions, protein-genome interactions, ordered association, or maturation-related changes could interfere with formation of a functional viral particle. Research in this area therefore connects structural mechanisms with viral replication and infectivity, helping identify which stages of particle production may be most relevant for antiviral intervention.
The organizing principles of capsid assembly extend beyond understanding natural viral replication. They support the design of viral vectors for gene delivery by informing how protective shells and genome-associated structures are constructed. The same principles also contribute to engineered nanostructures for biotechnology and medicine, where controlled protein organization can provide a useful design framework.