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Threonine 162 of hepatitis B virus core protein, the putative phosphorylation residue by protein kinase A, is important for HBV replication

Authors
Jung, Jaesung; Kim, Kyongmin
Department
Department of Microbiology
Abstract
Phosphorylation of Hepatitis B virus (HBV) C protein (HBc) at Ser157, Ser164, and Ser172 residues by serine/arginine protein-specific kinases (SRPK) or protein kinase C (PKC) have been demonstrated to modulate HBV replication. However, Thr162, Ser170, or Ser178 residues of HBc have been suggested as the putative phosphorylation sites possibly by the protein kinase A (PKA). To examine the importance of putative PKA phosphorylation sites of HBc, Thr162, Ser170, or Ser178 was mutated to alanine to mimic nonphosphorylated threonine/serine or to glutamic acid to mimic phosphoserine. HBV replicative intermediate DNA was significantly decreased by Thr162 to Ala (T162A) mutation, indicating that Thr 162 residue is important for HBV DNA synthesis. To further investigate the importance of other putative PKA phosphorylation sites in the presence or absence of T162A mutation, more HBc mutants were constructed. The HBV DNA synthesis was decreased more dramatically when mutants contain T162A mutations. In vivo phosphorylaiton assay also indicate that Thr 162 of HBc may be phosphorylated. Taken together, our results suggest that Thr 162 residue may be phosphorylated and modulate DNA replication.
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