Carboxyl-terminus of RNase H Contributes to Hepatitis B Virus Genome Replication
Jung, Jaesung; Lee, Hye-Jin; Kim, Kyongmin
Department of Microbiology, Ajou University School of Medicine
Multi-functional polymerase of hepatitis B virus (HBV) participates in pregenomic RNA (pgRNA) encapsidation and DNA synthesis, and acts as a primer for minus-strand DNA initiation. Previous studies have shown that RNase H domain of hepadnaviral polymerase may contribute to viral genome replication. Yet more studies are needed to precisely elucidate the roles of RNase H motifs and/or residues in HBV replications. In the present study, several RNase H mutants were constructed and analyzed. We found that nine mutants (L804D, L806T, Q809P, P810Y, T812P, G813L, R814S, T815K and A819I) are significantly reduced or defective in HBV DNA synthesis. Among these, Q809P and T815K mutants yielded barely non-detectable viral DNAs. Additional alanine substitution mutants showed that F808, T815, and L817 residues of RNase H may also contribute to HBV DNA synthesis. Unlike the Q809P mutant, Q809A mutant did not show any reduction in HBV DNA synthesis showing WT level, suggesting that structural changes of HBV RNase H may affect genome replication. Altogether we suggest that C-terminus of RNase H contributes to viral replication and further studies are underway to investigate the pgRNA encapsidation and minus-strand DNA synthesis by RNase H variants.
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