Abstract
As an example for studies of contacts involved in complex biological systems, peptide ligands that bind to the core antigen of hepatitis B virus (HBcAg) have been selected from a random hexapeptide library displayed on filamentous phage. Affinity-purified phage bearing aa sequence LLGRMK, or some related sequences, bound full-length or truncated HBcAg but did not bind denatured HBcAg. The long (L), but not the short (S), hepatitis B virus envelope polypeptide, when synthesized in an in vitro system, bound firmly to HBcAg, indicating that interaction between HBcAg and the pre-S region of the L polypeptide is critical for virus morphogenesis. This interaction was inhibited by peptide ALLGRMKG, suggesting that this and related small molecules may inhibit viral assembly.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacteriophages / metabolism*
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Base Sequence
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DNA Primers
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Hepatitis B Core Antigens / biosynthesis
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Hepatitis B Core Antigens / chemistry
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Hepatitis B Core Antigens / metabolism*
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Hepatitis B Surface Antigens / biosynthesis
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Hepatitis B Surface Antigens / chemistry
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Hepatitis B Surface Antigens / metabolism*
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Hepatitis B virus / metabolism*
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Ligands
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Oligopeptides / chemistry
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Oligopeptides / metabolism*
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Point Mutation
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Polymerase Chain Reaction
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Protein Biosynthesis
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Protein Structure, Secondary
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Random Allocation
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / metabolism
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Transcription, Genetic
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Viral Envelope Proteins / metabolism*
Substances
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DNA Primers
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Hepatitis B Core Antigens
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Hepatitis B Surface Antigens
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Ligands
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Oligopeptides
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Recombinant Proteins
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Viral Envelope Proteins