A peptide from the interaction site of VIM and N–P complex exhibits antiviral ability.

(A) Interaction between VIM mutants and the N–P complex. VIM head domain-related mutant (VIMΔ20, VIMΔ40, VIM60, and VIMΔ80) plasmids were transfected into HEK293T cells with N-Myc and HA–P plasmids. The cell lysates were subjected to an IP assay using anti-FLAG affinity gel. Lane 12 shows that the interaction between the N–P complex and VIMΔ80 mutant was lost. (B) Graphical representation of the results of (A). (C) Strep-20 full inhibited HPIV3 infection. Strep-20 full plasmid or strep-scramble plasmid was transfected into A549 cells prior to HPIV3 infection (MOI = 0.1). Cells underwent lysis, and HPIV3 HN protein, strep-tagged proteins, and GAPDH were detected. (D) Titer of HPIV3 in supernatants from HPIV3 infected A549 cells which were treated with 20 fullTAT peptide, and TAT was used as a control. (E) 20 fullTAT peptide inhibited HPIV3 replication. A549 cells were infected with HPIV3 before being treated with 20 fullTAT (HPIV3 MOI = 0.1). Both HPIV3 HN protein and viral RNA levels were detected. (F) Titer of hRSV in supernatants from hRSV infected A549 cells which were treated with 20 fullTAT peptide, and TAT was used as a control.(G) The 20 fullTAT peptide inhibited hRSV replication. A549 cells were infected with hRSV (MOI = 1) before being treated with 20 fullTAT peptide and TAT peptide. Viral P protein and RNA levels were detected. Values are means ± SDs from three experiments. For panels D, E, F, and G, Student’s t test was used, and * p value<0.05, ** p value<0.01, *** p value<0.001, **** p value<0.0001, and ns = not significant.