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J. Biol. Chem., Vol. 276, Issue 11, 8142-8148, March 16, 2001
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From the Institutes of Hepatitis delta virus (HDV) is a satellite
virus of hepatitis B virus, as it requires hepatitis B virus for
virion production and transmission. We have previously demonstrated
that sequences within the C-terminal 19-amino acid domain flanking the
isoprenylation motif of the large hepatitis delta antigen
(HDAg-L) are important for virion assembly. In this study,
site-directed mutagenesis and immunofluorescence staining demonstrated
that in the absence of hepatitis B virus surface antigen (HBsAg), the
wild-type HDAg-L was localized in the nuclei of transfected COS7 cells.
Nevertheless, in the presence of HBsAg, the HDAg-L became both nuclei-
and cytoplasm-distributed in about half of the cells. An HDAg-L mutant
with a substitution of Pro-205 to alanine could neither form HDV-like
particles nor shift the subcellular localization in the presence of
HBsAg. In addition, nuclear trafficking of HDAg-L in heterokaryons
indicated that HDAg-L is a nucleocytoplasmic shuttling protein. A
proline-rich HDAg peptide spanning amino acid residues 198 to 210, designated NES(HDAg-L), can function as a nuclear export signal (NES)
in Xenopus oocytes. Pro-205 is critical for the NES
function. Furthermore, assembly of HDV is insensitive to
leptomycin B, indicating that the NES(HDAg-L) directs nuclear export of
HDAg-L to the cytoplasm via a chromosome region maintenance
1-independent pathway.
A Novel Chromosome Region Maintenance 1-independent Nuclear
Export Signal of the Large Form of Hepatitis Delta Antigen That
Is Required for the Viral Assembly*
,
Biochemistry,
§ Microbiology, and ¶ Molecular Medicine, College of
Medicine, National Taiwan University, No. 1, Jen-Ai Rd., First
Section, Taipei, Taiwan
*
This work was supported by Research Grants NSC
89-2320-B-002-217 and NSC 89-2320-B-002-246 from the National Science
Council of the Republic of China.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.
To whom correspondence should be addressed. Tel.:
886-2-23123456, ext. 8217; Fax: 886-2-23915295; E-mail:
mfchang@ha.mc.ntu.edu.tw.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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