Inhibition of hepatitis B virus assembly with synthetic peptides derived from the viral surface and core antigens
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-HB...
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| Format: | Article |
| Language: | English English |
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Applied Microbiology, Molecular and Cellular Biosciences Research Foundation
2002
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| Online Access: | http://psasir.upm.edu.my/id/eprint/34512/1/Inhibition%20of%20hepatitis%20B%20virus%20assembly%20with%20synthetic%20peptides%20derived%20from%20the%20viral%20surface%20and%20core%20antigens.pdf http://psasir.upm.edu.my/id/eprint/34512/7/48_103.pdf http://psasir.upm.edu.my/id/eprint/34512/ https://www.jstage.jst.go.jp/article/jgam/48/2/48_2_103/_article |
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| Summary: | 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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