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Originally published In Press as doi:10.1074/jbc.M200613200 on June 11, 2002

J. Biol. Chem., Vol. 277, Issue 36, 33058-33067, September 6, 2002
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The Double-stranded RNA-activated Kinase, PKR, Can Phosphorylate Hepatitis D Virus Small Delta Antigen at Functional Serine and Threonine Residues*

Chi-Wu ChenDagger , Yeou-Guang Tsay§, Hui-Lin Wu, Chi-Hua LeeDagger , Ding-Shinn Chen, and Pei-Jer ChenDagger §||

From the Dagger  Graduate Institute of Microbiology and § Graduate Institute of Clinical Medicine, College of Medicine, National Taiwan University, Taipei, Taiwan and the  Hepatitis Research Center, National Taiwan University Hospital, Taipei, Taiwan

Hepatitis D virus (HDV) encodes two proteins, the 24-kDa small delta antigen (S-HDAg) and 27-kDa large delta antigen (L-HDAg) in its single open reading frame. Both of them had been identified as nuclear phosphoproteins. Moreover, the phosphorylated form of S-HDAg was shown to be important for HDV replication. However, the kinase responsible for S-HDAg phosphorylation remains unknown. Therefore, we employed an in-gel kinase assay to search candidate kinases and indeed identified a kinase with a molecular mass of about 68 kDa. Much evidence demonstrated this kinase to be the double-stranded RNA-activated kinase, PKR. The immunoprecipitated endogenous PKR was sufficient to catalyze S-HDAg phosphorylation, and the kinase activity disappeared in the PKR-depleted cell lysate. The S-HDAg and PKR could be co-immunoprecipitated together, and both of them co-located in the nucleolus. The LC/MS/MS analysis revealed that the serine 177, serine 180, and threonine 182 of S-HDAg were phosphorylated by PKR in vitro. This result was consistent with previous phosphoamino acid analysis indicating that serine and threonine were phosphorylation targets in S-HDAg. Furthermore, serine 177 was also shown to be the predominant phosphorylation site for S-HDAg purified the from cell line. In dominant negative PKR-transfected cells, the level of phosphorylated S-HDAg was suppressed, but replication of HDV was enhanced. Other than human immunodeficiency virus type 1 trans-activating protein (Tat), S-HDAg is another viral protein phosphorylated by PKR that may regulates HDV replication and viral response to interferon therapy.

* This work was supported in part by grants from the National Science Council, Executive Yuan, Taiwan.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.

|| Supported in part by an International Research Scholar grant from Howard Hughes Medical Institute. To whom correspondence should be addressed. Tel.: 886-02-23123456 (ext. 7072); Fax: 886-02-23317624; E-mail: peijer@ha.mc.ntu.edu.tw.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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