Ebola virus VP35 has novel NTPase and helicase-like activities

Shu, Ting; Gan, Tianyu; Bai, Peng; Wang, Xiaotong; Qian, Qi; Zhou, Hui; Cheng, Qi; Qiu, Yang; Yin, Lei; Zhong, Jin; Zhou, Xi

In addition, we further assessed the relation of the NT-Pase activity with the dsRNA-binding and helix-unwinding activities of VP35 by specifically blocking the NTPase activity of VP35 using AMP-PNP, the non-hydrolysable ATP analog. Consistent with our data by using MBP-VP35 137-173 , blocking the NTPase via AMP-PNP treatment efficiently blocked the helix-unwinding activity of MBP-VP35 in a dose-dependent manner ( Figure 6D ), but did not inhibit the dsRNA-binding activity ( Figure 6E ). Together, our data show that the NTPase activity is required for the helix-unwinding activity but not the dsRNA-binding activity of EBOV VP35.