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
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.
Download File
![[img]](http://psasir.upm.edu.my/34512/1.hassmallThumbnailVersion/Inhibition%20of%20hepatitis%20B%20virus%20assembly%20with%20synthetic%20peptides%20derived%20from%20the%20viral%20surface%20and%20core%20antigens.pdf)  Preview |
|
PDF (Abstract)
Inhibition of hepatitis B virus assembly with synthetic peptides derived from the viral surface and core antigens.pdf
Download (35kB)
| Preview
|
|
Additional Metadata
Actions (login required)
 |
View Item |