Fig. 6
From: Significance of hepatitis B virus capsid dephosphorylation via polymerase
Core dephosphorylation-deficient RNase H mutants exhibited a 10-fold reduction in viral infectivity. A & (B) A 10-fold reduction in HBc core protein signal was detected by confocal IFA in RNase H domain mutants deficient in putative phosphatase activity at 7 dpi. None of the pol mutation sites overlaps with the S envelope ORF. HepG2-NTCP-AS2 cells were in vitro infected with equal amounts of virions from WT-HBV and mutants defective in core dephosphorylation. MYR: a preS1 inhibitory control peptide. C The ELISA assays for HBsAg (left) and HBeAg (right) in the media detected a 10-fold reduction in cells infected with RNase H domain mutants. D RNase H domain mutant V686E exhibited a 2.5-fold reduction in attachment (left) and subsequent internalization (right). Naked capsids do not bind to NTCP and are present in near equal proportion in WT and mutant virions. HBV DNA was measured by qPCR. *** p < 0.001, p value refers to the Student’s t-test statistical analysis