Cloning, expression and display of the PreS domain of hepatitis B virus on filamentous bacteriophage M13

The PreS domain of hepatitis B virus (HBV) is believed to be involved in virion assembly and attachment to a hepatocyte receptor during infection. In order to study the functions of this region, we fused it to the g3p protein of bacteriophage M13 that allows the fusion protein to be displayed at the...

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Main Authors: Kok, W.L., Yusoff, K., Nathan, S., Tan, W.S.
Format: Article
Published: Informa UK Limited 2002
Online Access:http://psasir.upm.edu.my/id/eprint/115373/
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author Kok, W.L.
Yusoff, K.
Nathan, S.
Tan, W.S.
author_facet Kok, W.L.
Yusoff, K.
Nathan, S.
Tan, W.S.
author_sort Kok, W.L.
building UPM Institutional Repository
collection Online Access
description The PreS domain of hepatitis B virus (HBV) is believed to be involved in virion assembly and attachment to a hepatocyte receptor during infection. In order to study the functions of this region, we fused it to the g3p protein of bacteriophage M13 that allows the fusion protein to be displayed at the tip of the filament. The fusion protein was detected by the anti-E tag antibody on a Western blot. The polypeptide in a soluble form was produced by transfecting a non-suppressor E. coli host cell with the recombinant phagemid. The soluble protein was detected in cytoplasm, in the periplasmic space and also in the medium. The functional display of the PreS domain would provide an alternative means to study its interactions with the nucleocapsid and hepatocytes.
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institution Universiti Putra Malaysia
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publishDate 2002
publisher Informa UK Limited
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spelling upm-1153732025-03-03T08:19:32Z http://psasir.upm.edu.my/id/eprint/115373/ Cloning, expression and display of the PreS domain of hepatitis B virus on filamentous bacteriophage M13 Kok, W.L. Yusoff, K. Nathan, S. Tan, W.S. The PreS domain of hepatitis B virus (HBV) is believed to be involved in virion assembly and attachment to a hepatocyte receptor during infection. In order to study the functions of this region, we fused it to the g3p protein of bacteriophage M13 that allows the fusion protein to be displayed at the tip of the filament. The fusion protein was detected by the anti-E tag antibody on a Western blot. The polypeptide in a soluble form was produced by transfecting a non-suppressor E. coli host cell with the recombinant phagemid. The soluble protein was detected in cytoplasm, in the periplasmic space and also in the medium. The functional display of the PreS domain would provide an alternative means to study its interactions with the nucleocapsid and hepatocytes. Informa UK Limited 2002 Article PeerReviewed Kok, W.L. and Yusoff, K. and Nathan, S. and Tan, W.S. (2002) Cloning, expression and display of the PreS domain of hepatitis B virus on filamentous bacteriophage M13. The Journal of Biochemistry, Molecular Biology and Biophysics, 6 (1). pp. 55-58. ISSN 1025-8140 https://taylorandfrancis.com/ 10.1080/10258140290010241
spellingShingle Kok, W.L.
Yusoff, K.
Nathan, S.
Tan, W.S.
Cloning, expression and display of the PreS domain of hepatitis B virus on filamentous bacteriophage M13
title Cloning, expression and display of the PreS domain of hepatitis B virus on filamentous bacteriophage M13
title_full Cloning, expression and display of the PreS domain of hepatitis B virus on filamentous bacteriophage M13
title_fullStr Cloning, expression and display of the PreS domain of hepatitis B virus on filamentous bacteriophage M13
title_full_unstemmed Cloning, expression and display of the PreS domain of hepatitis B virus on filamentous bacteriophage M13
title_short Cloning, expression and display of the PreS domain of hepatitis B virus on filamentous bacteriophage M13
title_sort cloning, expression and display of the pres domain of hepatitis b virus on filamentous bacteriophage m13
url http://psasir.upm.edu.my/id/eprint/115373/
http://psasir.upm.edu.my/id/eprint/115373/
http://psasir.upm.edu.my/id/eprint/115373/