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Inhibition of hepatitis B virus assembly with synthetic peptides derived from the viral surface and core antigens


Citation

Tan, Wen Siang (2002) Inhibition of hepatitis B virus assembly with synthetic peptides derived from the viral surface and core antigens. Journal of General and Applied Microbiology, 48 (2). pp. 103-107. ISSN 0022-1260; ESSN: 1349-8037

Abstract / Synopsis

The long surface antigen (L-HBsAg) of hepatitis B virus (HBV) plays a central role in the production of infectious virions. During HBV morphogenesis, both the PreS and S domains of L-HBsAg form docking sites for the viral nucleocapsids. Thus, a compound that disrupts the interaction between the L-HBsAg and nucleocapsids could serve as a therapeutic agent against the virus based upon inhibition of morphogenesis. Synthetic peptides correspond to the binding sites in L-HBsAg inhibited the association of L-HBsAg with core antigen (HBcAg). A synthetic peptide carrying the epitope for a monoclonal antibody to the PreS1 domain competed weakly with L-HBsAg for HBcAg, but peptides corresponding to a linear sequence at the tip of the nucleocapsid spike did not, showing that the competing peptide does not resemble the tip of the spike.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Science and Environmental Studies
DOI Number: https://doi.org/10.2323/jgam.48.103
Publisher: Applied Microbiology, Molecular and Cellular Biosciences Research Foundation
Keywords: Hepatitis B virus; Inhibitors; Protein-protein interaction; Synthetic peptides
Depositing User: Nurul Ainie Mokhtar
Date Deposited: 19 Sep 2016 17:46
Last Modified: 19 Sep 2016 17:46
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.2323/jgam.48.103
URI: http://psasir.upm.edu.my/id/eprint/34512
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