Assembly of Epstein-Barr virus capsid in nucleus

The EBV capsid assembly includes major capsid proteins (VCA), minor capsid proteins (BORF1 and BDLF1), a small capsid protein (BFRF3) and scaffold proteins (BdRF1 and BVRF2). This study investigates how BFRF3 affects EBV capsid assembly and whether the protein binds to hexameric VCA as its homolog of herpes simplex virus type 1 (HSV-1) does on the hexameric major capsid protein, VP5. Our current study shows that the BFRF3 interacts with VCA. According to a sucrose gradient sedimentation study, we show that VCA forms higher order oligomer than VP5, which was monomer. When VCA and BFRF3 are co-expressed in 293T cells, VCA not only interacts with BFRF3 but also reduces the sizes of VCA oligomer; is disassembled and forms small oligomer. Furthermore, we also find that BFRF3 promote the translocation of VCA into nuclear. This study reveals that BFRF3 is critically involved in the process of capsid assembly.

Project ID:PG10301-0177
External Project ID:NHRI-EX103-10135BI