Abstract
The surface glycoprotein (G) of Borna disease virus (BDV) plays central roles in the process of viral entry. BDV G is cleaved by cellular furin-like proteases into two components, GP1 and GP2. Although GP1 is involved in the virus entry into cells, the binding activity of GP1 to cells is unknown. Therefore, we expressed the wild-type GP1 and a variety of GP1 deletion mutants that were FLAG-tagged at the C-terminus in human embryonic kidney 293T cells. These proteins were then purified using an anti-FLAG antibody and evaluated for their ability to bind to cell lines. GP1 bound to BDV-permissive cells but not to non-permissive cells. GP1 also inhibited BDV infection via its binding to cells. This binding assay should prove useful to map the receptor-binding domain of BDV.
