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

We then examined whether the RNA helix unwinding activity of VP35 is ATP-dependent. Our data showed that MBP-VP35 could only unwind the RNA helix in the presence of ATP ( Figure 2D, lane 4) , but not in the absence of ATP (lane 3) or the presence of AMP-PNP, a nonhydrolysable ATP analog (lane 5). Moreover, our results show that the presence of ATP can promote the helixunwinding activity of VP35 in a dose-dependent manner ( Figure 2E) . Additionally, all four types of NTPs could enable VP35 to unwind the RNA helix substrate, and the preference of the helix unwinding activity of VP35 on different NTPs is consistent with that of the VP35 NTPase, as CTP is the least favorable for both activities ( Figure 2F and Figure 1A) .