3,769
Views
49
CrossRef citations to date
0
Altmetric
Article Addendum

Ebolavirus VP35 is a multifunctional virulence factor

, , &
Pages 526-531 | Received 22 Jun 2010, Accepted 10 Jul 2010, Published online: 01 Nov 2010

Figures & data

Figure 1 Viral infection triggers the IFNβ signal transduction pathway of the host innate immune system, activating the antiviral state. Viral RNAs are detected by cytosolic helicases RIG-I/MDA-5, leading to the phosphorylation and nuclear translocation of transcription factor IR F3/7, which stimulates the production of the IFNβ cytokine. IFNβ activates the JAK/STAT pathway and IFN-stimulated response elements (ISREs) or antiviral genes, such as PKR, MHC class I and 2′5′ OAS.

Figure 1 Viral infection triggers the IFNβ signal transduction pathway of the host innate immune system, activating the antiviral state. Viral RNAs are detected by cytosolic helicases RIG-I/MDA-5, leading to the phosphorylation and nuclear translocation of transcription factor IR F3/7, which stimulates the production of the IFNβ cytokine. IFNβ activates the JAK/STAT pathway and IFN-stimulated response elements (ISREs) or antiviral genes, such as PKR, MHC class I and 2′5′ OAS.

Figure 2 Structure of ZEBOV VP35 IID (PDB: 3FKE). Ribbon representation of Zaire Ebola VP35 IID in two orientations, along with corresponding electrostatic surfaces that reveal the highly conserved nature of the (A) first basic patch and (B) central basic patch.

Figure 2 Structure of ZEBOV VP35 IID (PDB: 3FKE). Ribbon representation of Zaire Ebola VP35 IID in two orientations, along with corresponding electrostatic surfaces that reveal the highly conserved nature of the (A) first basic patch and (B) central basic patch.

Figure 3 Crystal structure of ZEBOV VP35 IID bound to dsRNA (PDB: 3L25). (A) Zaire Ebola VP35 IID in complex with dsRNA reveals two binding modes between protein and dsRNA. (B) The “end-cap” formed by residues at the intersubdomain interface mimic blunt end dsRNA recognition by RLRs. (C) Protein-protein interactions observed between different molecules in the crystal structure reveal previously unrecognized dsRNA-independent functions of VP35 IID.

Figure 3 Crystal structure of ZEBOV VP35 IID bound to dsRNA (PDB: 3L25). (A) Zaire Ebola VP35 IID in complex with dsRNA reveals two binding modes between protein and dsRNA. (B) The “end-cap” formed by residues at the intersubdomain interface mimic blunt end dsRNA recognition by RLRs. (C) Protein-protein interactions observed between different molecules in the crystal structure reveal previously unrecognized dsRNA-independent functions of VP35 IID.