Journal
MOLECULAR CELL
Volume 69, Issue 1, Pages 136-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2017.11.034
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Funding
- Novo Nordisk Foundation [NNF14CC0001]
- Danish Cancer Society [R72-A4351-13-S2, R124-A7827-15-S2]
- Deutsche Forschungsgemeinschaft (DFG) through Collaborative Research Center (CRC) [1021]
- German Center of Infection Research (DZIF)
- Novo Nordisk Fonden [NNF17OC0028080] Funding Source: researchfish
- The Danish Cancer Society [R124-A7657, R124-A7827, R72-A4351] Funding Source: researchfish
- Novo Nordisk Foundation Center for Protein Research [PI Jakob Nilsson, PI Guillermo Montoya] Funding Source: researchfish
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Transcription of the Ebola virus genome depends on the viral transcription factor VP30 in its unphosphorylated form, but the underlying molecular mechanism of VP30 dephosphorylation is unknown. Here we show that the Ebola virus nucleoprotein (NP) recruits the host PP2A-B56 protein phosphatase through a B56-binding LxxIxE motif and that this motif is essential for VP30 dephosphorylation and viral transcription. The LxxIxE motif and the binding site of VP30 in NP are in close proximity, and both binding sites are required for the dephosphorylation of VP30. We generate a specific inhibitor of PP2A-B56 and show that it suppresses Ebola virus transcription and infection. This work dissects the molecular mechanism of VP30 dephosphorylation by PP2A-B56, and it pinpoints this phosphatase as a potential target for therapeutic intervention.
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