Furthermore, an understanding of these specialized processes may generate experimental handles by which to study intractable features of the mechanism of conventional secretory and membrane protein biogenesis. Molecular chaperones involved in viral capsid assembly Recently, we established a cell-free system in which authentic empty Hepatitis B viral capsids were assembled de novo upon translation of the core polypeptide. Using this system we find that Hepatitis B viral capsid assembly proceeds via a previously unknown intermediate that appears to contain molecular chaperones. The isolated intermediate can be manipulated with energy substrates to generate capsids. We are currently pursuing the implications of these findings as both a tool for understanding host molecular chaperone machines and the processes of viral assembly and dissembly for both Hepatitis B virus and Human Immunodeficiency Virus.
B mediates stopping and restarting of translocation.
Evidence for an alternate model of human P-glycoprotein structure and biogenesis. A eukaryotic cytosolic chaparonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle. J. Cell Biology.