Virus Core Disassembly
Virus Core Disassembly - Related Videos
02:42
In Vitro Disassembly of the Influenza A Virus Core Using pH-Controlled Gradient Centrifugation
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2026
Source: Stauffer, S. et al. In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation. J. Vis. Exp. (2016)This video demonstrates the pH-dependent disassembly of influenza A virus (IAV) cores using gradient ultracentrifugation. It outlines glycerol gradient preparation, ultracentrifugation, and how different pH conditions affect IAV core disassembly.
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.
02:49
Detection of Biofilm Disassembly Through a Dispersion Assay
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2025
The video showcases a biofilm dispersion assay using a multi-well plate. Buffer and glucose treatment disassemble the biofilm, releasing bacteria, while bile salts induce stress, retaining bacteria in the protective extracellular polymeric substance. Higher dispersion with buffer and glucose confirms successful biofilm disassembly, estimated by colony forming units measurement.
02:23
Visualizing the Effect of pH on Solubilization of the Influenza A Viral Core
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2026
Source: Stauffer, S. et al., In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation. J. Vis. Exp. (2016)This video demonstrates the effect of pH on the solubilization of influenza A viral cores. Gel electrophoresis and protein staining reveal the progressive disassembly of the core structure under acidic conditions.
01:35
Disassembly of Intermediate Filaments
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2023
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs. Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
FAQs
Acidification or receptor engagement can destabilize viral structures and initiate conformational rearrangements. These structural changes alter interactions within the core or capsid, preparing the particle for genome release. Because the triggers can depend on the host-cell environment, their timing and location help determine whether unpackaging occurs productively during infection.
Membrane conditions can promote structural transitions that culminate in membrane fusion, allowing viral contents to cross into the host-cell interior. Fusion is therefore linked to the physical environment surrounding the particle, rather than occurring independently of entry. When coordinated with core destabilization, it supports delivery of the genome and associated proteins to the appropriate intracellular site.
Proteolytic processing can modify viral or associated proteins as the particle transitions from a stable extracellular form to an active intracellular complex. By changing protein structure or interactions, this processing may contribute to destabilization and genome release. Its importance lies in coupling molecular rearrangement with the timing of infection, helping prevent premature activation before entry.
Disassembly must occur in a cellular setting that permits genome delivery while limiting exposure to cellular defenses. If unpackaging is coordinated with entry and intracellular trafficking, the released genome can proceed toward replication. Studying where and when this transition occurs therefore helps explain differences in infectivity and how viruses manage the balance between particle stability and intracellular activation.
Investigations focus on the conditions that destabilize viral structures, including pH, receptor binding, membrane conditions, and host-cell factors. Researchers compare these influences with the timing and location of genome release and associated protein changes. This approach connects structural transitions to infection outcomes and clarifies how a virus moves from an extracellular particle to an active intracellular complex.
Disassembly research identifies stages at which viral structures become dependent on specific environmental cues or host-cell factors. Those stages can inform antiviral strategies designed to interfere with genome delivery or activation. The same knowledge supports vaccine development by clarifying structural features and transitions that are relevant to how viral particles interact with host cells.