Biochemical and genetic tests have revealed that a liver protein called NTCP is a functional receptor for hepatitis B and D viruses, which should lead to an improved understanding of the infections caused by these viruses and assist the development of new intervention strategies.

The combination of in vitro investigations, the zebrafish screening model and rodent experiments offered a unique approach to optimizing nanoparticles modified with Hepatitis B virus-derived peptides to specifically target hepatocytes.

A novel and potent receptor-binding-blockage human neutralizing antibody prevents HBV infection, and suppresses HBV infection therapeutically in HBV-infected mice.

The putative substrate pantoate binds to a sodium-coupled secondary transporter of the bile acid sodium symporter family, with sodium-dependent binding and conformational changes consistent with an elevator mechanism of transport.

The mechanism triggering HBV membrane fusion involves ERp57, a cellular protein disulfide isomerase, and ultimately leads to the exposition of a fusion peptide that was identified in the pre-S1 determinant.