Post-translational modification of delta antigen of hepatitis D virus
Journal
Current Topics in Microbiology and Immunology
Journal Volume
307
Pages
91-112
Date Issued
2006
Author(s)
Abstract
The hepatitis delta virus (HDV) genome has only one open reading frame, which encodes the viral small delta antigen. After RNA editing, the same open reading frame is extended 19 amino acids at the carboxyl terminus and encodes the large delta antigen. These two viral proteins escort the HDV genome through different cellular compartments for the complicated phases of replication, transcription and, eventually, the formation of progeny virions. To orchestrate these events, the delta antigens have to take distinct cues to traffic to the right compartments and make correct molecular contacts. In eukaryotes, post-translational modification (PTM) is a major mechanism of dictating the multiple functions of a single protein. Multiple PTMs, including phosphorylation, isoprenylation, acetylation, and methylation, have been identified on hepatitis delta antigens. In this chapter we review these PTMs and discuss their functions in regulating and coordinating the life cycle of HDV. ? Springer-Verlag 2006.
SDGs
Other Subjects
arginine; casein kinase II; cysteine; hepatitis delta antigen; lysine; methyltransferase; protein farnesyltransferase; protein kinase C; protein kinase R; protein p300; serine; threonine; virus enzyme; virus RNA; hepatitis delta antigen; acetylation; amino acid sequence; carboxy terminal sequence; eukaryote; genome analysis; Hepatitis delta virus; human; life cycle; nonhuman; open reading frame; priority journal; progeny; protein function; protein methylation; protein phosphorylation; protein processing; regulatory mechanism; review; RNA editing; virion; virus genome; biosynthesis; methylation; molecular genetics; phosphorylation; virus replication; Eukaryota; Hepatitis delta virus; Acetylation; Amino Acid Sequence; Hepatitis delta Antigens; Methylation; Molecular Sequence Data; Phosphorylation; Protein Isoprenylation; Protein Processing, Post-Translational; Virus Replication
Publisher
Springer Verlag
Type
review