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Article

Structure of the Ebola VP35 interferon inhibitory domain

2 Jan 2009

Abstract excerpt

Ebola viruses (EBOVs) cause rare but highly fatal outbreaks of viral hemorrhagic fever in humans, and approved treatments for these infections are currently lacking. The Ebola VP35 protein is multifunctional, acting as a component of the viral RNA polymerase complex, a viral assembly factor, and an inhibitor of host interferon (IFN) production. Mutation of select basic residues within the C-terminal half of VP35...

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Hepatitis B Virus Studies
Viral Infections and Outbreaks Research
Viral Infections and Vectors

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 19122151
DOI: 10.1073/pnas.0807854106

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Structure of the Ebola VP35 interferon inhibitory domainPMID 19122151Read ↗

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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.Semantic proximity Read ↗

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