Document 0291
 DOCN  M95A0291
 TI    The pre-S domain of the large viral envelope protein determines host
       range in avian hepatitis B viruses.
 DT    9510
 AU    Ishikawa T; Ganem D; Howard Hughes Medical Institute, University of
       California Medical; Center, San Francisco 94143-0502, USA.
 SO    Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6259-63. Unique Identifier :
       AIDSLINE MED/95327626
 AB    In addition to their well-recognized hepatotropism, all hepatitis B
       viruses (HBVs) display marked species specificity, growing poorly or not
       at all in species other than those closely related to their natural
       hosts. We have examined the molecular basis for this narrow host range,
       using duck HBV (DHBV) and heron HBV (HHBV) as a model system. HHBV
       virions will not infect ducks in vivo and infect cultured duck
       hepatocytes extremely inefficiently in vitro. Mutant HHBV genomes
       lacking all viral envelope proteins (HHBV env-) can be complemented in
       trans with DHBV envelope proteins; the resulting pseudotyped virions can
       efficiently infect duck hepatocytes. Further complementation analysis
       reveals that of the two viral surface proteins (L and S), it is the L
       protein that determines host range. Pseudotyping of HHBV env- with
       DHBV/HHBV chimeric envelope proteins reveals that replacement of as few
       as 69 amino acids of the pre-S domain of the HHBV L protein by their
       DHBV counterparts is sufficient to permit infection of duck hepatocytes.
       These studies indicate that the species-specificity of hepadnaviral
       infection is determined at the level of virus entry and is governed by
       the pre-S domain of the viral L protein.
 DE    Amino Acid Sequence  Animal  Birds/*VIROLOGY  Chimera  Codon
       Comparative Study  Ducks/VIROLOGY  Gene Products,
       env/GENETICS/*PHYSIOLOGY  Genes, Viral
       Hepadnaviridae/GENETICS/PHYSIOLOGY/*PATHOGENICITY  Hepatitis B
       Virus/GENETICS/*PHYSIOLOGY/*PATHOGENICITY  Molecular Sequence Data
       Mutagenesis, Site-Directed  *Point Mutation  Polymerase Chain Reaction
       Sequence Homology, Amino Acid  Species Specificity  Support, Non-U.S.
       Gov't  Support, U.S. Gov't, P.H.S.  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).