Assembly of Epstein-Barr virus capsid in nucleus

Capsid assembly by the Epstein-Barr virus (EBV) is a complex process that involves the formation of a scaffold by BVRF2 and BdRF1 in the nucleus. The scaffold serves as a platform, on which capsid proteins, i.e. BDLF1, BORF1, VCA, and BFRF3, form an icosahedral capsid shell. Therefore, the scaffold and capsid proteins must be conveyed to the nucleus from the cytoplasm for capsid assembly. However, the location of capsid assembly in the nucleus and the underlying mechanism of this assembly are unclear. Our current work demonstrates that EBV capsid is assembled close to the promyelocytic leukemia nuclear bodies (PML-NBs). Hence, the first aim of this investigation is to study how EBV capsid proteins are conveyed to the sites of capsid assembly and how PML-NBs interact with these proteins to affect capsid assembly. The second aim of this study is to elucidate how the two scaffold proteins, BVRF2 and BdRF1, are translocated to the assembly sites to form a scaffold that has an optimal size for capsid assembly. The last aim of this investigation is to determine how BFRF3, a protein that binds to the tip of hexons on a capsid, affects capsid assembly. This investigation will ultimately reveal the mechanism by which the EBV capsid is formed in the nucleus, knowledge of which process is crucial to understanding the EBV lytic cycle.

Project ID:PG10201-0119
External Project ID:NHRI-EX102-10135BI