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J. Biol. Chem., Vol. 276, Issue 27, 25166-25175, July 6, 2001
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From the Hepatitis delta virus (HDV) encodes two isoforms
of delta antigens (HDAgs). The small form of HDAg is required for HDV
RNA replication, while the large form of HDAg inhibits the viral
replication and is required for virion assembly. In this study, we
found that the expression of B23, a nucleolar phosphoprotein involved
in disparate functions including nuclear transport, cellular
proliferation, and ribosome biogenesis, is up-regulated by these two
HDAgs. Using in vivo and in vitro experimental
approaches, we have demonstrated that both isoforms of HDAg can
interact with B23 and their interaction domains were identified as the
NH2-terminal fragment of each molecule encompassing the
nuclear localization signal but not the coiled-coil region of HDAg.
Sucrose gradient centrifugation analysis indicated that the majority of
small HDAg, but a lesser amount of the large HDAg, co-sedimented with
B23 and nucleolin in the large nuclear complex. Transient transfection
experiments also indicated that introducing exogenous full-length B23,
but not a mutated B23 defective in HDAg binding, enhanced HDV RNA
replication. All together, our results reveal that HDAg has two
distinct effects on nucleolar B23, up-regulation of its gene expression
and the complex formation, which in turn regulates HDV RNA replication.
Therefore, this work demonstrates the important role of nucleolar
protein in regulating the HDV RNA replication through the complex
formation with the key positive regulator being small HDAg.
The Nucleolar Phosphoprotein B23 Interacts with
Hepatitis Delta Antigens and Modulates the Hepatitis Delta Virus RNA
Replication*
,
Institute of Biochemistry and
¶ Institute of Microbiology and Immunology, National Yang-Ming
University, Taipei, 112 and the § Department of
Pharmacology, College of Medicine, Chang Gung University,
Taipei, Taiwan, Republic of China
*
This work was supported by grants DOH87-HR-502,
DOH88-HR-502, NHRI-GT-EX89B502L, NHRI-GT-EX89B502Ls, and
NHRI-EX90-9002BL from the National Health Research Institute and in
part by Grants NSC88-2315-B-010-007MH and NSC89-2315B-010-006MH from
the National Science Council, and a grant from Medical Research and
Advancement of Foundation in memory of Dr. Chi-Sheu Tsou (to Y.-H.
W. L.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of a National Chair Award from the Ministry of
Education (1998-2001) and Distinguished Investigator of National Science Council (1996-2002), Republic of China. To whom correspondence should be addressed: Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan. Tel.: 886-2-2826-7124; Fax:
886-2-2826-4843; E-mail: yhwulee@ym.edu.tw.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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