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Threonine 162 of hepatitis B virus core protein is important for genome replication

Jung, Jaesung; Kim, Kyongmin
Department of Microbiology, Ajou University School of Medicine
Serines 157, 164, and 172 of hepatitis B virus (HBV adw) core (C) protein were demonstrated to be phosphorylated by several host kinases, such as serine/arginine protein-specific kinases and/or protein kinase C, and to modulate HBV replications at various steps. Although three additional Thr162, Ser170, and Ser178 residues in the conserved RRxS/T motif of HBV (adw) C protein have been suggested as putative protein kinase A phosphorylation sites, actual phosphorylations and the contributions on replications have not been elucidated. Thr162, Ser170, and Ser178 can be phosphorylated in vivo which is the first demonstration that Thr162 is phosphorylated. To elucidate the contributions on HBV replication, these Ser/Thr residues were mutated to Ala or Glu to mimic nonphosphorylated Ser/Thr or phosphorylated Ser/Thr, respectively. In general, Ser/Thr to Ala mutations cause significant replication defect compared to Ser/Thr to Glu mutations. Among those, Thr162 to Ala (T162A) mutation decreased replicative intermediate DNA synthesis significantly. However, Ser178 to Glu or Ala mutations did not decrease HBV DNA synthesis. HBV DNA synthesis was decreased more dramatically by double-point mutants in the presence of T162A mutation, indicating that Thr162 may contribute to HBV DNA replication.
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