Cellular nuclear export factors TAP and Aly are required for HDAg-L-mediated assembly of hepatitis delta virus
Journal
Journal of Biological Chemistry
Journal Volume
291
Journal Issue
50
Pages
26226-26238
Date Issued
2016
Author(s)
Abstract
was replaced by Ala. HDAg-L was found to colocalize with TAP and Aly in the nucleus. The C-terminal domain of HDAg-L was shown to directly interact with the N terminus of TAP, whereas an HDAg-L mutant lacking the NLS failed to interact with full-length TAP. In addition, small hairpin RNA-mediated down-regulation of TAP or Aly reduced nuclear export of HDAg-L and assembly of HDV virions. Furthermore, a peptide, TAT-HDAg-L(198-210), containing the 10-amino acid TAT peptide and HDAg-L(198-210), inhibited the interaction between HDAg-L and TAP and blocked HDV virion assembly and secretion. These data demonstrate that formation and release of HDV particles are mediated by TAP and Aly.
SDGs
Publisher
American Society for Biochemistry and Molecular Biology Inc.
Type
journal article