Capsid Stability Analysis

Capsid stability analysis is the study of how effectively a virus’s protein shell maintains its structure and protects the viral genome under defined conditions. Researchers assess disassembly and structural changes by varying factors such as pH, temperature, ionic strength, or chemical exposure, then measuring particle integrity and infectivity. In immunology and infection research, these measurements clarify how viruses persist outside host cells, enter susceptible cells, and withstand immune or environmental pressures. Stability profiles can guide vaccine formulation, antiviral development, viral vector design, and assessments of transmission risk, linking molecular structure to infection outcomes.

Capsid Stability Analysis - Related Videos

Research

JoVE Journal - Immunology and Infection

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.

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.

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.

Research

JoVE Journal - Immunology and Infection
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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.

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.

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