Fig. 1: The enzymatic activity of NiV L-P complex.

a Size-exclusion chromatography and SDS-PAGE profiles of NiV L-P complex. Molecular weights (in kilodaltons, kDa) of protein maker are shown on the left, and the L and P bands are indicated on the right. At least three independent experiments were performed with similar results. b De novo transcription activity of NiV L-P complex. The 3’-end 96 nt sequence of NiV genome was chemically synthesized and used as the template. The micrograph was representative of three independent experiments using different protein preparations, all of which showed similar results. c Capping activity of NiV L-P complex. The 5’-triphosphorylated mRNA sequence of 5’UTR of N gene was generated by in vitro transcription using T7 RNA polymerase and used as the capping substrate. Data are representative of two independent experiments using different protein preparations, and both experiments showed similar results. d Methyltransferase activity of NiV L-P complex. The cap structure at the 5’-end of Gppp-RNA was formed by the Vaccinia virus capping enzyme, and Gppp-RNA was a better substrate for methyltransferase than ppp-RNA. The data represented mean values (histograms) ±s.d (error bars) of three independent experiments (n = 3). Source data are provided as a Source Data file. NiV Nipah virus.