Related Experiment Videos
[Expression of thermal stable, soluble hepatitis E virus recombinant antigen]
Mingcheng Zhang1, Yao Yi, Meiyun Zhan
1Hepatitis Branch, Institute of Virology,Chinese Academy of Preventive Medicine, Beijing 100052, China.
Summary
A novel thioredoxin fusion expression system successfully produced a soluble, thermally stable, and biologically active hepatitis E virus (HEV) recombinant antigen, crucial for diagnostic development.
Area of Science:
- Recombinant protein expression
- Virology
- Biochemistry
Context:
- Hepatitis E virus (HEV) poses a significant global health challenge.
- Developing stable and active recombinant antigens is critical for accurate diagnostics.
- Current expression systems may face limitations in producing functional viral antigens.
Purpose:
- To develop a robust method for expressing a thermally stable and soluble HEV recombinant antigen.
- To utilize the thioredoxin fusion system for enhanced protein expression and stability.
- To confirm the biological activity and antigenicity of the expressed HEV protein.
Summary:
- The thioredoxin fusion expression system was employed to express a specific HEV ORF2 gene fragment in E. coli.
- The expressed thioredoxin-HEV fusion protein demonstrated high expression levels, solubility, and thermal stability after heat treatment.
- Enzyme-linked immunosorbent assay (ELISA) confirmed the HEV-specific antigenicity of the purified recombinant protein.
Impact:
- Successful expression of a stable, soluble, and active HEV antigen facilitates improved diagnostic test development.
- This method offers a promising strategy for producing other challenging viral antigens.
- Enhanced antigen stability can lead to more reliable and longer-lasting diagnostic reagents.