Core protein: A pleiotropic keystone in the HBV lifecycle

摘要: Hepatitis B Virus (HBV) is a small virus whose genome has only four open reading frames. We argue that the simplicity of virion correlates with complexity functions for viral proteins. focus on HBV core protein (Cp), (183 residue) self-assembles to form capsid. However, its are little more complicated than that. In an infected cell Cp modulates almost every step lifecycle. bound nuclear DNA and affects epigenetics. RNA specificity. assembles specifically reverse transcriptase-viral complex or, apparently, nothing at all. Indeed been one model systems investigation self-assembly. participates in regulation transcription. signals completion transcription support secretion. carries both localization surface antigen (HBsAg) binding sites; these appear be regulated by contents can targeted antivirals - while self-assembly most accessible activities, we it makes sense engage broader spectrum function. This article forms part symposium Antiviral Research "From discovery Australia development new curative therapies hepatitis B: unfinished story."