Identification The Binding Domain Of PLSCR1 That Interact With HBV

Hepatitis B virus (HBV), the prototype for the family Hepadnaviridae, is known as the smallest DNA virus that infects human beings. HBV infection causes acute and chronic necroinflammatory liver disease. Infected individuals are at high risk of developing liver cirrhosis and eventually, hepatocellular carcinoma.LS was the main reason on damage ,die and dissolve of hepatocyte. The HBV infection and replication can be inhibited by some host Protein-LS interaction .Phospholipid scramblase 1 (PLSCR1) is a calcium-binding, multiply palmitoylated type II endofacial plasma membrane protein, while unpalmitoylated PLSCR1 protein can import into the nucleus, where it binds to genomic DNA. Although the original work showed that PLSCR1 contributes to the transbilayer movement of phospholipids.In summary, we reached the interaction between PLSCR1 and LS, and studied its biological significance in the process. Preliminary findings of this study, exogenous PLSCR1 inhibits secretion of HBsAg, after sub-expression, we found that the inhibition of some fragments of PLSCR1 on HBsAg was more significant than the full-length. The results may provide further evidence for potential roles of PLSCR1 ,and for the possibility of PLSCR1 as a new potential target for anti-HBV drugs.