Inhibition of duck hepatitis B virus infection by a myristoylated pre-S peptide of the large viral surface protein.

Abstract

We have used the duck hepatitis B virus (DHBV) model to study the interference with infection by a myristoylated peptide representing an N-terminal pre-S subdomain of the large viral envelope protein. Although lacking the essential part of the carboxypeptidase D (formerly called gp180) receptor binding site, the peptide binds hepatocytes and subsequently blocks DHBV infection. Since its activity requires an amino acid sequence involved in host discrimination between DHBV and the related heron HBV (T. Ishikawa and D. Ganem, Proc. Natl. Acad. Sci. USA 92:6259-6263, 1995), we suggest that it is related to the postulated host-discriminating cofactor of infection.

• Authors: Stephan Urban, Philippe Gripon
• Journal: Journal of virology (J Virol) Vol. 76 Issue 4 Pg. 1986-90 (Feb 2002) ISSN: 0022-538X [Print] United States
• PMID: 11799193 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Peptides
• Pre-S protein, Duck hepatitis B virus
• Viral Envelope Proteins
• Myristic Acid

Topics

• Amino Acid Sequence
• Animals
• Ducks
• Hepadnaviridae Infections (virology)
• Hepatitis B Virus, Duck (genetics, metabolism, pathogenicity)
• Hepatitis, Viral, Animal (virology)
• Hepatocytes (virology)
• Molecular Sequence Data
• Myristic Acid (metabolism)
• Peptides (chemistry, genetics, metabolism)
• Viral Envelope Proteins (chemistry, genetics, metabolism)