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Updated: Aug 30, 2026

Modeling Hepatitis B Virus Infection in Non-Hepatic 293T-NE-3NRs Cells
Published on: June 5, 2020
In vitro and in vivo interactions between the hepatitis B virus protein P22 and the cellular protein gC1qR
S Lainé1, A Thouard, J Derancourt
1Laboratoire de Génétique et Biologie Cellulaire, Université de Versailles St. Quentin, Versailles, France.
Abstract:
gC1qR, a mitochondrial matrix protein, was identified as the main cellular partner of the hepatitis B virus P22 protein. We demonstrated by immunofluorescence studies that some P22 molecules were colocalized with the endogenous gC1qR in both the cytoplasm and the nucleus but never in the mitochondria. We also showed that the last 34 amino acids of P22 were involved in the association with gC1qR.
Insights
Hepatitis B virus P22 protein interacts with gC1qR, a mitochondrial matrix protein. This interaction occurs in the cytoplasm and nucleus, not mitochondria, involving P22's C-terminal region.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- The hepatitis B virus (HBV) P22 protein is a viral component implicated in viral replication and pathogenesis.
- gC1qR (Complement C1q Receptor) is primarily known as a mitochondrial matrix protein involved in cellular processes.
Purpose of the Study:
- To identify cellular partners of the hepatitis B virus P22 protein.
- To investigate the subcellular localization of the interaction between P22 and its cellular partner.
Main Methods:
- Immunofluorescence studies were employed to visualize the colocalization of proteins within cells.
- Biochemical assays were used to determine the specific protein domains involved in the interaction.
Main Results:
- gC1qR was identified as the primary cellular binding partner for the HBV P22 protein.
- Colocalization of P22 and gC1qR was observed in the cytoplasm and nucleus, but notably absent from mitochondria.
- The C-terminal 34 amino acids of the P22 protein were found to be essential for its association with gC1qR.
Conclusions:
- The hepatitis B virus P22 protein interacts with gC1qR, a protein typically localized to the mitochondrial matrix.
- The interaction between P22 and gC1qR occurs in extranuclear cellular compartments (cytoplasm and nucleus), suggesting a role beyond mitochondrial function.
- The C-terminal region of P22 is critical for mediating this interaction, providing insights into the molecular mechanism of P22-gC1qR binding.
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