N-terminally His-tagged hepatitis B core antigens: construction, expression, purification and antigenicity
The core antigen of the hepatitis B virus (HBcAg) has been used widely as a diagnostic reagent for the identification of the viral infection. However, purification using the conventional sucrose density gradient ultracentrifugation is time consuming and costly. To overcome this, HBcAg particles disp...
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| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2009
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| Online Access: | http://psasir.upm.edu.my/id/eprint/15854/1/N-terminally%20His-tagged%20hepatitis%20B%20core%20antigens%20%20construction%2C%20expression%2C%20purification%20and%20antigenicity.pdf http://psasir.upm.edu.my/id/eprint/15854/ |
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| Institution: | Universiti Putra Malaysia |
| Language: | English |
| Summary: | The core antigen of the hepatitis B virus (HBcAg) has been used widely as a diagnostic reagent for the identification of the viral infection. However, purification using the conventional sucrose density gradient ultracentrifugation is time consuming and costly. To overcome this, HBcAg particles displaying His-tag on their surface were constructed and produced in Escherichia coli. The recombinant His-tagged HBcAgs were purified using immobilized metal affinity chromatography. Transmission electron microscopy and enzyme-linked immunosorbent assay (ELISA) revealed that the displayed His-tag did not impair the formation of the core particles and the antigenicity of HBcAg. |
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