Fig. 1
From: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses
Binding of Henipavirus W proteins to importins. The NLS regions of Henipavirus W proteins bind with high affinity and specificity to the importin α2 subfamily containing importin α3 and α4. a The W proteins contain the Soyouz module moiety (Soyouz) and PCT disordered (Paramyxo_PCT) regions, which are conserved across paramyxovirus phosphoproteins. However, the W proteins of HeV and NiV W also possess a unique C terminus compared with other P gene products and contain an NLS that mediates translocation of W into the nucleus. b HeV W and NiV W interact with importin α3 and α4. Co-immunoprecipitation assay performed with Flag antibody on lysates of HEK293T cells expressing Flag-tagged importin α1, α3, α4, α5, α6, α7 and HA-tagged full length HeV W and NiV W, as indicated. Western blots were performed for HA and Flag. WCL, whole cell lysate; IP, immunoprecipitation. pCAGGS denotes empty vector control. c The NLS region of HeV W and NiV W interact with high affinity to importin α3. An ELISA was performed using GST-W (GST as a negative control) proteins coated on 96-well plates, and binding of 6xHis-tagged importin α1, α3, α7 assessed using an anti-6xHis HRP antibody. Error bars show the S.E.M for three replicates. d MST assay confirms high affinity binding of importin α3 to the NLS region of NiV W proteins, and comparatively lower affinity binding to importin α1 and α7
