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Detection of Neutralization-sensitive Epitopes in Antigens Displayed on Virus-Like Particle (VLP)-Based Vaccines Using a Capture Assay
Published on: February 10, 2022
Engineering Viral Surface Antigens to Improve Display on Virus-like Particle (VLP) Vaccine Prototypes
Mona Pißarreck1,2, Kristina Katsoutas1,2, Jörn Stitz1
1Research Group Pharmaceutical Biotechnology, Faculty of Applied Natural Sciences, TH Köln University of Applied Sciences, Campusplatz 1, 51379 Leverkusen, Germany.
Biotech (Basel (Switzerland))
|June 25, 2026
Summary
Engineering viral spike proteins with modified tails enhances their display on virus-like particles (VLPs) for improved vaccine development. A truncated tail from GaLV TM showed the best incorporation into HIV Gag VLPs, preserving key functions.
Area of Science:
- Virology
- Vaccinology
- Protein Engineering
Background:
- Virus-like particles (VLPs) are promising vaccine platforms for displaying viral antigens.
- Efficient antigen display density on VLPs is crucial for robust immune responses.
- SARS-CoV-2 spike protein variants were engineered to improve VLP surface decoration.
Purpose of the Study:
- To engineer SARS-CoV-2 spike protein variants with modified cytoplasmic tails (CTs) for enhanced VLP incorporation.
- To evaluate the functionality and immunogenicity of these engineered spike proteins displayed on HIV Gag-derived VLPs.
- To prototype chimeric HIV-SARS-CoV-2 particles as vaccine components.
Main Methods:
- Flow cytometry and Western blot to assess protein expression and VLP incorporation.
- Syncytia-formation assays and lentiviral vector titration to evaluate fusogenicity and cell entry.
- Immunoprecipitation with neutralizing antibodies to confirm epitope display.
Main Results:
- All engineered spike variants were expressed, recruited receptors, mediated membrane fusion, and decorated VLPs and extracellular vesicles (EVs).
- A spike variant with a truncated gibbon ape leukemia virus (GaLV) transmembrane (TM) protein CT demonstrated superior incorporation into HIV Gag VLPs.
- All variants presented a neutralization-sensitive epitope within the receptor-binding domain.
Conclusions:
- Engineering of viral antigen CTs can significantly enhance VLP decoration efficiency.
- Essential ectodomain functions, including receptor binding and fusogenicity, are preserved.
- The truncated GaLV TM CT shows potential for improving the display of other viral antigens on various membrane-enveloped VLPs.
