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Updated: Aug 14, 2026

Expression and Purification of Virus-like Particles for Vaccination
Published on: June 2, 2016
[Expression in Escherichia coli and immunogenicity of rotavirus VP7]
1Institute of Medical Biology, CAMS & PUMC, Kunming 650118, China. Liuyongsd@21cn.com
Insights
Researchers developed a new rotavirus vaccine candidate. The VP7 outer capsid protein was expressed as a fusion protein, generating virus-binding and neutralizing antibodies in animal models.
Area of Science:
- Virology
- Vaccinology
- Molecular Biology
Background:
- Rotaviruses are a leading cause of severe diarrhea in children globally.
- The VP7 outer capsid protein is crucial for rotavirus vaccines.
- Developing effective subunit or recombinant vaccines is a priority.
Purpose of the Study:
- To express a functional part of the rotavirus VP7 gene.
- To create a chimeric protein for potential vaccine development.
- To assess the immunogenicity of the expressed protein.
Main Methods:
- The VP7 gene segment encoding antigenic regions was cloned into E. coli.
- A fusion protein with glutathione S-transferase (GST) was expressed.
- The chimeric protein's reactivity with antibodies and its ability to generate immune responses were evaluated.
Main Results:
- The chimeric VP7-GST protein was successfully expressed in E. coli.
- The fusion protein reacted with polyclonal antibodies against whole rotavirus.
- Immunization of rabbits and mice with the purified protein elicited virus-binding and neutralizing antibodies.
Conclusions:
- The expressed VP7 fusion protein is a promising candidate for rotavirus subunit or recombinant vaccines.
- The study demonstrates the potential of using recombinant DNA technology to produce vaccine antigens.
- Further studies are warranted to evaluate the efficacy of this candidate in preventing rotavirus infections.
Abstract:
Rotaviruses are the single most important cause of severe diarrhea in young children all over the world. VP7 is the major outer capsid and is a primary candidate for inclusion in a subunit or recombinant vaccine. Part of the VP7 gene containing all the three antigenic regions was expressed as a chimeric protein with glutathione S-transferase (GST) in E. coli. The chimeric protein, representing about 30% of the total protein of the recombinant-plasmid-carrying bacteria, reacted with polyclonal antibodies raised against whole virus. Immunization of sero-negative rabbits and mice with purified fusion-protein generated both virus-binding and neutralizing antibodies.
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