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Parvovirus B19 VP2-proteins produced in Saccharomyces cerevisiae: comparison with VP2-particles produced by
1Institute of Medical Microbiology, University of Regensburg, Regensburg, Germany.
Abstract:
The capsids of human parvovirus B19 consist of two structural proteins, the minor-capsid protein VP1 and the major-capsid protein VP2. The latter which constitutes for 95% of the capsid are able to form virus-like particles (VLPs) in yeast without the presence of VP1-proteins. VP2-proteins produced in Saccharomyces cerevisiae have the capacity to form VLPs in the absence of VP1-proteins. These yeast-derived VLPs resemble native virus or recombinant VP2-VLPs produced by baculovirus systems in respect of size, molecular weight and of antigenicity as shown by antigen-capture ELISA and T-cell proliferation tests. Regarding costs, yield and ease of handling particle production in yeast represents an alternative to the recombinant baculovirus expression system which is so far the source for VP2-VLPs of human parvovirus B19.
Insights
Human parvovirus B19 capsids can be produced as virus-like particles (VLPs) using yeast. Yeast-derived VP2-VLPs are comparable to those from baculovirus systems, offering a cost-effective alternative.
Area of Science:
- Virology
- Biotechnology
- Protein Expression
Background:
- Human parvovirus B19 (B19) capsids are composed of VP1 and VP2 proteins.
- VP2 protein constitutes 95% of the capsid and can self-assemble into virus-like particles (VLPs).
- Current production of VP2-VLPs relies on baculovirus expression systems.
Purpose of the Study:
- To investigate the production of B19 VP2-VLPs in yeast.
- To compare yeast-derived VP2-VLPs with those produced by established methods.
Main Methods:
- Production of VP2 proteins in Saccharomyces cerevisiae (yeast).
- Formation and characterization of yeast-derived VLPs.
- Analysis of VLP size, molecular weight, and antigenicity using antigen-capture ELISA and T-cell proliferation assays.
Main Results:
- Yeast successfully produced VP2 proteins capable of forming VLPs without VP1.
- Yeast-derived VP2-VLPs exhibited similar size, molecular weight, and antigenicity to native B19 or baculovirus-produced VLPs.
- Antigenicity was confirmed through antigen-capture ELISA and T-cell proliferation tests.
Conclusions:
- Yeast is a viable system for producing human parvovirus B19 VP2-VLPs.
- Yeast-based production offers advantages in terms of cost, yield, and ease of handling compared to baculovirus systems.
- This presents a promising alternative for generating B19 VP2-VLPs for research and potential therapeutic applications.
