Inhibition of duck hepatitis B virus infection by a myristoylated pre-S peptide of the large viral surface protein.
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.
Urban
Stephan
S
Zentrum für Molekulare Biologie, Universität Heidelberg (ZMBH), 69120 Heidelberg, Germany. s.urban@med.uni-heidelberg.de
Gripon
Philippe
P
D000595:Amino Acid Sequence; D000818:Animals; D004372:Ducks; D018347:Hepadnaviridae Infections / Q000821:virology; D015611:Hepatitis B Virus, Duck / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity*; D006524:Hepatitis, Viral, Animal / Q000821:virology; D022781:Hepatocytes / Q000821:virology*; D008969:Molecular Sequence Data; D019814:Myristic Acid / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D010455:Peptides; C077433:Pre-S protein, Duck hepatitis B virus; D014759:Viral Envelope Proteins; D019814:Myristic Acid