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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

VP35  -  polymerase complex protein

Reston ebolavirus

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Disease relevance of VP35

  • This system was used to exchange the EBOV Zaire and EBOV Reston nucleocapsid (NC) proteins NP, VP35, VP30, and L, which catalyze replication and transcription [1].

High impact information on VP35

  • Importantly, we show that the recombinant viruses were attenuated for growth in cell culture and that they activated IRF-3 and IRF-3-inducible gene expression at levels higher than that for Ebola virus containing wild-type VP35 [2].
  • In the context of Ebola virus pathogenesis, VP35 may function to limit early IFN-beta production and other antiviral signals generated from cells at the primary site of infection, thereby slowing down the host's ability to curb virus replication and induce adaptive immunity [2].
  • We now show that VP35 inhibits virus infection-induced transcriptional activation of IFN regulatory factor 3 (IRF-3)-responsive mammalian promoters and that VP35 does not block signaling from the IFN-alpha/beta receptor [3].
  • Exchange of NP, VP35, and L between the two replication systems did not lead to detectable reporter gene expression [4].
  • A 22-mer P-PMO designed to base pair with the translation start site region of EBOV VP35 positive-sense RNA generated sequence-specific and time- and dose-dependent inhibition of EBOV amplification in cell culture [5].

Biological context of VP35

  • The ebolavirus VP35 protein antagonizes the cellular type I interferon response by blocking phosphorylation of IRF-3, a transcription factor that turns on the expression of a large number of antiviral genes [6].
  • To identify the domain of VP35 responsible for interferon antagonism, we generated mutations within the VP35 gene and found that a C-terminal basic amino acid motif is required for inhibition of ISG56 reporter gene expression as well as IFN-beta production [6].


  1. A reconstituted replication and transcription system for Ebola virus Reston and comparison with Ebola virus Zaire. Boehmann, Y., Enterlein, S., Randolf, A., Mühlberger, E. Virology (2005) [Pubmed]
  2. Reverse genetic generation of recombinant Zaire Ebola viruses containing disrupted IRF-3 inhibitory domains results in attenuated virus growth in vitro and higher levels of IRF-3 activation without inhibiting viral transcription or replication. Hartman, A.L., Dover, J.E., Towner, J.S., Nichol, S.T. J. Virol. (2006) [Pubmed]
  3. The Ebola virus VP35 protein inhibits activation of interferon regulatory factor 3. Basler, C.F., Mikulasova, A., Martinez-Sobrido, L., Paragas, J., Mühlberger, E., Bray, M., Klenk, H.D., Palese, P., García-Sastre, A. J. Virol. (2003) [Pubmed]
  4. Comparison of the transcription and replication strategies of marburg virus and Ebola virus by using artificial replication systems. Mühlberger, E., Weik, M., Volchkov, V.E., Klenk, H.D., Becker, S. J. Virol. (1999) [Pubmed]
  5. VP35 knockdown inhibits Ebola virus amplification and protects against lethal infection in mice. Enterlein, S., Warfield, K.L., Swenson, D.L., Stein, D.A., Smith, J.L., Gamble, C.S., Kroeker, A.D., Iversen, P.L., Bavari, S., Mühlberger, E. Antimicrob. Agents Chemother. (2006) [Pubmed]
  6. A C-terminal basic amino acid motif of Zaire ebolavirus VP35 is essential for type I interferon antagonism and displays high identity with the RNA-binding domain of another interferon antagonist, the NS1 protein of influenza A virus. Hartman, A.L., Towner, J.S., Nichol, S.T. Virology (2004) [Pubmed]
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