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Western Blotting

Western Blotting

Western blotting is an analytical technique for protein identification. It has various applications in immunology and medicine, including detecting diseases like bovine spongiform encephalopathy, mad cow disease, and human and feline immunodeficiency virus from biological samples.
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Development of a Hepatitis B Virus Reporter System to Monitor the Early Stages of the Replication Cycle

Development of a Hepatitis B Virus Reporter System to Monitor the Early Stages of the Replication Cycle

Published on: February 1, 2017

Label-Free Tracking of Hepatitis B Virus Core Protein Capsid Assembly in Real-Time Using Protein Charge Transfer

Shah Ekramul Alom¹, Karthik Swaminathan¹, V Nuzelu¹

¹Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati 781039, Assam, India.

Biomacromolecules

|June 20, 2024

Summary

A new label-free method, protein charge transfer spectra (ProCharTS), tracks Hepatitis B virus (HBV) capsid assembly in real-time. This technique offers a simple, sensitive alternative to expensive methods for studying viral protein assembly.

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Author Spotlight: Advancements and Challenges in Hepatitis B Virus Detection

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Area of Science:

Biophysics
Structural Biology
Virology

Background:

Hepatitis B virions are double-shelled particles with nucleocapsids formed by Hepatitis B virus core protein (HBV Cp) homodimers.
HBV Cp and its domain HBV Cp149 self-assemble into capsids (T=4 or T=3) under high salt conditions.
Traditional methods for studying HBV capsid assembly are often expensive and complex.

Purpose of the Study:

To introduce a simple, robust, and label-free technique for real-time monitoring of Hepatitis B virus capsid assembly.
To demonstrate the utility of protein charge transfer spectra (ProCharTS) for studying HBV Cp assembly dynamics.

Main Methods:

Utilized protein charge transfer spectra (ProCharTS) to monitor HBV capsid assembly in real-time.
ProCharTS absorption arises from photoinduced electron transfer between charged amino acid residues (glutamate, lysine, arginine, histidine).
Employed anisotropy-based fluorescence assay to characterize assembled capsids versus dimers.

Main Results:

ProCharTS absorption and luminescence showed a time-dependent sigmoidal increase during HBV capsid formation, indicating amplified charge transfer upon dimer assembly.
The ProCharTS signal correlated with the generation of new contacts at the dimer-dimer interface during capsid assembly.
Anisotropy-based fluorescence assay confirmed increased structural order in assembled capsids compared to native or unfolded dimers.

Conclusions:

Protein charge transfer spectra (ProCharTS) provide a sensitive, label-free tool for rapid, real-time tracking of HBV capsid assembly.
ProCharTS can effectively characterize assembled capsids and differentiate them from unassembled dimers.
This method offers a cost-effective and accessible alternative for studying viral capsid formation.