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Originally published In Press as doi:10.1074/jbc.M010087200 on April 17, 2001

J. Biol. Chem., Vol. 276, Issue 27, 25166-25175, July 6, 2001
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The Nucleolar Phosphoprotein B23 Interacts with Hepatitis Delta Antigens and Modulates the Hepatitis Delta Virus RNA Replication*

Wen-Hung HuangDagger , Benjamin Y. M. Yung§, Wan-Jr Syu, and Yan-Hwa Wu LeeDagger ||

From the Dagger  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

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.

* 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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