Extended Data Figure 7: The impact of diverse RNase III members on virus infection.
From: RNase III nucleases from diverse kingdoms serve as antiviral effectors
a, Schematic depicting core domains of human Drosha, C-terminal region of C. intestinalis Drosha, or full-length RNase III of S. pombe, M. maripaludis, and S. pyogenes. Domains depicted include Proline-rich (P-rich), arginine–serine-rich (RS-rich), conserved central domain (CED), RNaseIII domain (RIIID), and double-stranded RNA binding domain (dsRBD). b, Western blots from BSR-T7 cells, co-transfected with the indicated RNase-III-expression plasmids and SeV rescue plasmids encoding SeV-GFP genome, SeV-N, SeV-P, and SeV-L genes. RNase III expression was determined at 48 h.p.t. and virus replication at 72 h.p.t. c, Western blot of DL1 cells treated with indicated dsRNA for 3 days and subsequently infected with SINV (MOI = 1) for 96 h. d, HEK293T (WT) or RNaseIII−/− cells were infected with SINV for 24 h. Graphs depict the number of SINV reads mapping to indicated positions along the viral genomes from the small RNA deep sequencing performed in Extended Data Fig. 1b.
