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Updated: Aug 9, 2026
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Isolation And Dendritic Cell-Uptake of Small Extracellular Vesicles from Echinococcus granulosus
Published on: March 28, 2025
[Expression, purification and identification of Echinococcus granulosus recombinant antigen B]
Xin-hua Chen1, Hao Wen, Xiao-mei Lu
1Surgical Lab, The First Affiliated Hospital, Medical School, Zhejiang Universtiy, Hangzhou, China.
Summary
Researchers purified recombinant hydatid disease antigen B using molecular methods. This purified antigen B can be used for monoclonal antibody production and phage antibody library screening.
Area of Science:
- Molecular biology
- Immunology
- Biochemistry
Context:
- Hydatid disease is a parasitic infection caused by Echinococcus tapeworms.
- Accurate diagnosis and effective treatment of hydatid disease rely on specific antigens.
- Recombinant antigen production offers a standardized and scalable source of diagnostic and therapeutic targets.
Purpose:
- To develop a method for purifying recombinant antigen B (AgB) from hydatid disease.
- To identify the molecular characteristics and specificity of the purified recombinant AgB.
- To establish a tool for advancing hydatid disease diagnostics and therapeutics.
Summary:
- A recombinant plasmid (pMalc2x-AgB) was expressed in E. coli to produce a fusion protein (rAgB-MBP).
- Factor Xa protease was used to cleave the maltose binding protein (MBP) from antigen B.
- Purification was achieved through affinity chromatography using amylose and hydroxyapatite columns, yielding pure rAgB (12,000 Mr).
- Western blotting confirmed the specificity of the purified rAgB by its ability to bind to specific antibodies in patient sera.
Impact:
- Enables the production of a well-defined recombinant antigen B for hydatid disease research.
- Facilitates the development of improved diagnostic tools, such as ELISAs and Western blots.
- Provides a crucial component for screening and producing monoclonal antibodies and for phage antibody library applications in hydatid disease research.
