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J Biol Chem, Vol. 273, Issue 13, 7650-7656, March 27, 1998
From the Institutes of Hepatitis delta antigens (HDAgs) are important
for the replication and assembly of hepatitis delta virus (HDV). To
understand the association between HDAgs and cellular proteins and the
mechanism of viral multiplication, we have studied the interaction
between HDAgs and nucleolin, a major nucleolar phosphoprotein. The
interaction between HDAgs and nucleolin was first demonstrated by
immunofluorescence staining studies. HDAgs and endogenous nucleolin
were colocalized in the nucleoli of cultured cells transfected with
plasmids encoding the small and large HDAg. Coimmunoprecipitation
results indicated that the NH2-terminal domain of
HDAg was essential for its binding to nucleolin. In vitro
ligand binding assays revealed two nucleolin binding sites, NBS1 and
NBS2. Each spanned amino acid residues 35-50 and 51-65, respectively,
with a conserved core sequence K(K/R)XK. HDV replication
was modulated by exogenous human nucleolin. In addition, a small HDAg
mutant S-d65/75, which possesses both NBS1 and NBS2, was capable of
transactivating HDV replication, whereas the small HDAg mutant
S-d50/75, which retained NBS1 but not NBS2, was unable to support the
replication of HDV. Thus, the nucleolin binding activity of HDAg is
critical for its nucleolar targeting and is involved in the modulation
of HDV replication.
The Nucleolin Binding Activity of Hepatitis Delta Antigen Is
Associated with Nucleolus Targeting
,, and
Biochemistry and
§ Microbiology, College of Medicine, National Taiwan
University, Taipei, Taiwan
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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