The Ebola Virus Nucleoprotein Recruits the Host PP2A-B56 Phosphatase to Activate Transcriptional Support Activity of VP30
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The Ebola Virus Nucleoprotein Recruits the Host PP2A-B56 Phosphatase to Activate Transcriptional Support Activity of VP30. / Kruse, Thomas; Biedenkopf, Nadine; Hertz, Emil Peter Thrane; Dietzel, Erik; Stalmann, Gertrud; López-Méndez, Blanca; Davey, Norman E; Nilsson, Jakob; Becker, Stephan.
In: Molecular Cell, Vol. 69, No. 1, 04.01.2018, p. 136-145.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - The Ebola Virus Nucleoprotein Recruits the Host PP2A-B56 Phosphatase to Activate Transcriptional Support Activity of VP30
AU - Kruse, Thomas
AU - Biedenkopf, Nadine
AU - Hertz, Emil Peter Thrane
AU - Dietzel, Erik
AU - Stalmann, Gertrud
AU - López-Méndez, Blanca
AU - Davey, Norman E
AU - Nilsson, Jakob
AU - Becker, Stephan
N1 - Copyright © 2017 Elsevier Inc. All rights reserved.
PY - 2018/1/4
Y1 - 2018/1/4
N2 - 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.
AB - 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.
U2 - 10.1016/j.molcel.2017.11.034
DO - 10.1016/j.molcel.2017.11.034
M3 - Journal article
C2 - 29290611
VL - 69
SP - 136
EP - 145
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 1
ER -
ID: 187554374