Considerable differences are observed in the global dissemination patterns of HBV-D and HBV-A, the genotypes of which have putative origins in North Africa/Middle East (HBV-D) and the Middle East/Central Asia (HBV-A).

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.

Small molecule antivirals that drive assembly of HBV capsid protein can also bind to pre-assembled capsids causing them to change morphology or even break, suggesting a complex transduction of binding effects across the capsid.

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

Duck Hepatitis B core protein forms capsids with a slowly folding extension domain which folding competence is important for viral replication.

The entry glycoproteins of hepatitis C virus, E1E2, possess a novel regulatory mechanism in which protein disorder is harnessed to control their activity and their ability to evade antibodies.

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.

All-atom molecular dynamics of the HBV capsid supports a role for structural asymmetry in biological function, reveals the potential for triangular pores to mediate cellular signaling, and indicates that capsid flexibility may limit resolution attainable by cryo-EM.