HBV p22-interacting protein C1QBP inhibits viral replication through impeding nucleocapsid formation and nuclear import.

ABSTRACT: The circulating hepatitis B virus (HBV) e antigen (HBeAg) is known to subvert the host immune system to benefit chronic HBV infection. However, the biological function of a major intracellular form of HBeAg, specifically the precore protein intermediate of 22 kDa (p22) lacking the N-terminal signal peptide, remains largely unclear. Through pull-down and mass spectrometry analysis, we re-identified the complement C1q binding protein (C1QBP) as a p22-binding protein. Immunofluorescence results demonstrated that C1QBP was predominantly localized in the mitochondrial matrix and the leaked C1QBP interacted with p22 in the cytosol. Using co-immunoprecipitation assay, we mapped the arginine-rich, highly positively charged C-terminal domain (CTD) of p22 and the internal domain aa 74-160 of C1QBP a

SUBMITTER: Peng X 

PROVIDER: S-EPMC12533850 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature