| Autor: |
Böttcher, B., Tsuji, N., Takahashi, H., Dyson, M. R., Zhao, S., Crowther, R. A., Murray, K. |
| Předmět: |
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| Zdroj: |
EMBO Journal; 12/1/98, Vol. 17 Issue 23, p6839-6845, 7p |
| Abstrakt: |
Peptides selected to bind to hepatitis B virus (HBV) core protein block interaction with the long viral surface antigen (L-HBsAg) in vitro. High resolution electron cryomicroscopy showed that one such peptide binds at the tips of the spikes of the core protein shell. The peptides contain two basic residues; changing either of two acidic residues at the spike tip to an alanine greatly reduced the binding affinity. Transfection of hepatoma cells with a replication-competent HBV plasmid gave significantly reduced production of virus in the presence of peptide, in a dose-dependent manner. These experiments show that the interaction of L-HBsAg with core particles is critical for HBV assembly, and give proof of principle for its disruption in vivo by small molecules. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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