Abstract
The initial binding of a virus to a target cell is a critical determinant of cell and tissue tropism, and thus of pathogenesis. Flaviviruses have a relatively simple structure with only a single envelope protein, making it likely that the motif responsible for target cell binding is expressed by the ectodomain of the envelope protein. Heparan sulfate (HS) are present in the extracellular matrix and/or tissue cell surface and involved in infection of JEV virus. Thus, the heparin binding activity of JEV may play an important role in its function on cellular surfaces. In the present study, we attempted to identify which of the basic residue contribute to the heparin binding of E279 to E297. We had created several mutants by substituting basic residues (K279, K286, R288, K290) with alanine in the putative heparin-binding regions. We also analyze the heparin binding affinity through fluorescence and NMR methods. The completion of this study will provide a structural basis for design of vaccines.