Rotavirus Dlps
Rotavirus Dlps - Related Videos
03:43
Plasmid-Mediated Generation of Recombinant Rotavirus in Cultured Cells
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2026
Source: Philip, A. A., et al. Simplified Reverse Genetics Method to Recover Recombinant Rotaviruses Expressing Reporter Proteins. J. Vis. Exp. (2020)This video demonstrates the recovery of recombinant rotavirus by transfecting plasmids encoding viral genome segments into hamster kidney cells, followed by amplification in monkey epithelial cells, enabling studies of rotavirus biology, replication, and vaccine development.
03:44
Isolation and Visualization of Rotavirus Genome via Gel Electrophoresis
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2026
Source: Philip, A. A., et al., Simplified Reverse Genetics Method to Recover Recombinant Rotaviruses Expressing Reporter Proteins. J. Vis. Exp. (2020)This video demonstrates the isolation of rotavirus double-stranded RNA from clarified cell lysates. It further illustrates the separation and visualization of genome segments through polyacrylamide gel electrophoresis.
03:30
Assessing Rotavirus Growth Curve by Plaque Assay
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2026
Source: Kadoya, S., Sano, D. Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus. J. Vis. Exp. (2019).This video demonstrates the use of a plaque assay to assess the rotavirus growth curve. The method involves infecting host cells with diluted virus, overlaying with agarose to restrict spread, and staining to visualize plaques formed by viral replication. By counting plaque-forming units at defined time points, the resulting growth curve reveals the lag, exponential, and...
04:12
Visualizing Trypsin-Activated Rotavirus Infection Using a Plaque Assay
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2026
Source: Philip, A. A., et. al., Simplified Reverse Genetics Method to Recover Recombinant Rotaviruses Expressing Reporter Proteins. J. Vis. Exp. (2020)This video demonstrates a plaque assay technique to monitor rotavirus infection in epithelial cells. Trypsin activation enhances viral entry, and staining highlights viable cells, enabling visualization of infection-induced plaques.
10:49
Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus
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Cited by 5 •
2019
Here we present two protocols, one for measuring the specific growth rate and the other for the cell-binding ability of rotavirus using the plaque assay and RT-qPCR. These protocols are available for confirming the differences in phenotypes between rotavirus strains.
FAQs
VP2 establishes the inner scaffold, while VP6 assembles as the surrounding layer to create concentric shells. This division of structural roles allows researchers to examine how individual proteins contribute to capsid organization rather than treating the particle as an undifferentiated structure. In bioengineering studies, the arrangement provides a defined system for investigating protein structure and assembly.
The absence of the outer proteins required for host-cell entry prevents the particles from functioning as infectious rotavirus structures. That distinction supports controlled laboratory research while preserving important inner-capsid features. Consequently, investigators can study capsid organization, protein interactions, and selected virus-host interaction questions without working with a particle designed for entry into host cells.
Their defined two-layer architecture and stability are central advantages for bioengineering. Because the particles reproduce key features of the rotavirus inner capsid while remaining noninfectious, researchers can use them as consistent platforms for examining structural organization and protein behavior. These properties also support efforts to adapt particle-based systems for vaccine, diagnostic, or delivery-related research.
They can support studies of capsid assembly, protein structure, and virus-host interactions. The VP2 and VP6 shells provide a tractable structural context in which the relationship between capsid components can be examined. This makes the particles relevant when researchers need to connect molecular organization with broader questions about how rotavirus structures interact with biological systems.
Their noninfectious character, stability, and defined inner-capsid structure make them useful starting points for vaccine and diagnostic research. The particles can provide a controlled rotavirus-related platform without relying on outer proteins required for host-cell entry. In these applications, researchers can focus on particle properties and structural features relevant to development rather than infectious behavior.
The platform may also support engineered particle-based delivery systems, in addition to vaccine and diagnostic assays. Its stable, noninfectious structure offers a controlled basis for exploring how rotavirus-derived particles can be used in engineered designs. These applications connect fundamental analysis of VP2 and VP6 organization with practical efforts to develop functional particle technologies.