Glyceraldehyde-3-Phosphate Dehydrogenase of Is a Plasminogen- and Actin-Binding Protein.

, an intraerythrocytic protozoa, can cause an emerging tick-borne disease-Human babesiosis. The parasite can successfully invade host red blood cells owing to the assistance of molecules expressed by babesia. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the housekeeping intracellular glycolytic enzyme, can also be expressed in the external of cells, where contributes to binding to several molecules such as plasminogen and actin. In the present study, we identified GAPDH (BmGAPDH) and generated the recombinant BmGAPDH (rBmGAPDH) via an expression system. Furthermore, we confirmed its catalytic dehydration activity . Moreover, we also demonstrated that rBmGAPDH could bind to human plasminogen and mouse α-actin. In addition, we demonstrated that rBmGAPDH could recognize anti- mouse serum. In conclusion, BmGAPDH is a multifunctional glycolytic enzyme, which can bind to host plasminogen and α-actin.