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pubmed-article:9843489pubmed:abstractTextPeptides 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.lld:pubmed
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pubmed-article:9843489pubmed:articleTitlePeptides that block hepatitis B virus assembly: analysis by cryomicroscopy, mutagenesis and transfection.lld:pubmed
pubmed-article:9843489pubmed:affiliationMedical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.lld:pubmed
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