Histone H1e interacts with small hepatitis delta antigen and affects hepatitis delta virus replication
Journal
Virology
Journal Volume
375
Journal Issue
1
Pages
197-204
Date Issued
2008
Author(s)
Abstract
Hepatitis delta virus (HDV) encodes two isoforms of delta antigens (HDAgs). The small form of HDAg (SHDAg) is required for HDV RNA replication, while the large form of HDAg (LHDAg) is required for viral assembly. Using tandem affinity purification method combined with mass spectrometry, we found that linker histone H1e bound to SHDAg. The binding domain of SHDAg to histone H1e was mapped to the N-terminal 67 amino acids. Oligomerization of SHDAg was required for its interaction with histone H1e. LHDAg barely bound to histone H1e and was masked at N-terminus. The binding domain of histone H1e to SHDAg was mapped to its central globular domain. HDV replication was inhibited by N- or C-terminal deletion mutants of histone H1e and was rescued by wild-type histone H1e. We conclude that histone H1e plays a significant role in HDV replication through forming protein complex with SHDAg. ? 2008 Elsevier Inc. All rights reserved.
SDGs
Other Subjects
amino acid; hepatitis delta antigen; histone H1; histone h1e; animal cell; article; controlled study; deletion mutant; Hepatitis delta virus; human; human cell; mass spectrometry; nonhuman; nucleotide sequence; oligomerization; priority journal; protein domain; purification; virus replication; Animals; Cell Line; Cercopithecus aethiops; Chromatography, Affinity; Hepatitis delta Antigens; Hepatitis Delta Virus; Histones; Humans; Mass Spectrometry; Protein Binding; Protein Interaction Domains and Motifs; Protein Interaction Mapping; Sequence Deletion; Virus Replication; Hepatitis delta virus
Type
journal article