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Affinity-purified sHBsAg-based virus-like particles as a platform for foreign mRNA binding
Karolina Gackowska1, Martyna Krejmer-Rabalska1, Karolina Drazkowska2
1Laboratory of Recombinant Vaccines, Intercollegiate Faculty of Biotechnology of University of Gdansk and Medical University of Gdansk, University of Gdansk, Poland.
Virology
|August 15, 2025
Summary
Hepatitis B virus (HBV) core protein motifs were engineered into HBV surface antigen virus-like particles (VLPs). These modified VLPs can self-assemble and bind mRNA, offering a novel platform for vaccine development.
Area of Science:
- Virology
- Vaccinology
- Biotechnology
Background:
- Virus-like particles (VLPs) are effective immunogens for preventing infectious diseases.
- Hepatitis B virus surface antigen (sHBsAg) VLPs self-assemble into immunogenic structures used in human vaccines.
- Chimeric sHBsAg VLPs can tolerate sequence alterations, making them versatile vaccine platforms.
Purpose of the Study:
- To investigate if introducing hepatitis B virus core protein (HBcAg) motifs into sHBsAg VLPs enables mRNA packing.
- To assess the impact of modifications for mRNA binding on VLP self-assembly.
- To evaluate the mRNA binding capacity of engineered sHBsAg VLPs.
Main Methods:
- Engineering sHBsAg VLPs with HBcAg motifs in cytosolic loops.
- Introducing a Twin-Strep-tag for enhanced purification.
- Assessing VLP self-assembly and mRNA binding capabilities.
Main Results:
- Engineered sHBsAg VLPs generally retained self-assembly ability despite modifications for mRNA binding.
- One modification resulted in a loss of self-assembly.
- Recombinant proteins demonstrated successful binding to various mRNAs.
- Twin-Strep-tag facilitated efficient and specific purification.
Conclusions:
- Modified sHBsAg VLPs can be engineered to pack mRNA while maintaining self-assembly.
- These findings present a novel VLP platform with potential applications in mRNA-based vaccines or delivery systems.
- Further research can explore the utility of these mRNA-packing VLPs.
