Ebola virus VP35 interaction with dynein LC8 regulates viral RNA synthesis

Priya Luthra; David S. Jordan; Daisy W. Leung; Gaya K. Amarasinghe; Christopher F. Basler

doi:10.1128/JVI.03652-14

Ebola virus VP35 interaction with dynein LC8 regulates viral RNA synthesis

Priya Luthra, David S. Jordan, Daisy W. Leung, Gaya K. Amarasinghe, Christopher F. Basler

Research output: Contribution to journal › Article › peer-review

41 Scopus citations

Abstract

Ebola virus VP35 inhibits alpha/beta interferon production and functions as a viral polymerase cofactor. Previously, the 8-kDa cytoplasmic dynein light chain (LC8) was demonstrated to interact with VP35, but the functional consequences were unclear. Here we demonstrate that the interaction is direct and of high affinity and that binding stabilizes the VP35 N-terminal oligomerization domain and enhances viral RNA synthesis. Mutational analysis demonstrates that VP35 interaction is required for the functional effects of LC8.

Original language	English
Pages (from-to)	5148-5153
Number of pages	6
Journal	Journal of virology
Volume	89
Issue number	9
DOIs	https://doi.org/10.1128/JVI.03652-14
State	Published - 2015

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abstract = "Ebola virus VP35 inhibits alpha/beta interferon production and functions as a viral polymerase cofactor. Previously, the 8-kDa cytoplasmic dynein light chain (LC8) was demonstrated to interact with VP35, but the functional consequences were unclear. Here we demonstrate that the interaction is direct and of high affinity and that binding stabilizes the VP35 N-terminal oligomerization domain and enhances viral RNA synthesis. Mutational analysis demonstrates that VP35 interaction is required for the functional effects of LC8.",

author = "Priya Luthra and Jordan, {David S.} and Leung, {Daisy W.} and Amarasinghe, {Gaya K.} and Basler, {Christopher F.}",

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AU - Jordan, David S.

AU - Leung, Daisy W.

AU - Amarasinghe, Gaya K.

AU - Basler, Christopher F.

PY - 2015

Y1 - 2015

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AB - Ebola virus VP35 inhibits alpha/beta interferon production and functions as a viral polymerase cofactor. Previously, the 8-kDa cytoplasmic dynein light chain (LC8) was demonstrated to interact with VP35, but the functional consequences were unclear. Here we demonstrate that the interaction is direct and of high affinity and that binding stabilizes the VP35 N-terminal oligomerization domain and enhances viral RNA synthesis. Mutational analysis demonstrates that VP35 interaction is required for the functional effects of LC8.

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Ebola virus VP35 interaction with dynein LC8 regulates viral RNA synthesis

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