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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my.upm.eprints.158542016-11-30T08:09:12Z http://psasir.upm.edu.my/id/eprint/15854/ N-terminally His-tagged hepatitis B core antigens: construction, expression, purification and antigenicity Yap, Wei Boon Tey, Beng Ti Ng, Michelle Yeen Tan Ong, Swee Tin Tan, Wen Siang 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. Elsevier 2009-09 Article PeerReviewed application/pdf en 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 Yap, Wei Boon and Tey, Beng Ti and Ng, Michelle Yeen Tan and Ong, Swee Tin and Tan, Wen Siang (2009) N-terminally His-tagged hepatitis B core antigens: construction, expression, purification and antigenicity. Journal of Virological Methods, 160 (1-2). pp. 125-131. ISSN 0166-0934; ESSN: 1879-0984 10.1016/j.jviromet.2009.04.038 |
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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. |
format |
Article |
author |
Yap, Wei Boon Tey, Beng Ti Ng, Michelle Yeen Tan Ong, Swee Tin Tan, Wen Siang |
spellingShingle |
Yap, Wei Boon Tey, Beng Ti Ng, Michelle Yeen Tan Ong, Swee Tin Tan, Wen Siang N-terminally His-tagged hepatitis B core antigens: construction, expression, purification and antigenicity |
author_facet |
Yap, Wei Boon Tey, Beng Ti Ng, Michelle Yeen Tan Ong, Swee Tin Tan, Wen Siang |
author_sort |
Yap, Wei Boon |
title |
N-terminally His-tagged hepatitis B core antigens: construction, expression, purification and antigenicity |
title_short |
N-terminally His-tagged hepatitis B core antigens: construction, expression, purification and antigenicity |
title_full |
N-terminally His-tagged hepatitis B core antigens: construction, expression, purification and antigenicity |
title_fullStr |
N-terminally His-tagged hepatitis B core antigens: construction, expression, purification and antigenicity |
title_full_unstemmed |
N-terminally His-tagged hepatitis B core antigens: construction, expression, purification and antigenicity |
title_sort |
n-terminally his-tagged hepatitis b core antigens: construction, expression, purification and antigenicity |
publisher |
Elsevier |
publishDate |
2009 |
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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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