Journal
JOURNAL OF VIROLOGY
Volume 89, Issue 9, Pages 5148-5153Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.03652-14
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Funding
- NIH [R01AI107056, R01AI059536, U19AI109945, U19AI109664, U19 AI070489, R01AI081914, T32-CA09547-37]
- Roche Translation and Clinical Research grant in infectious diseases
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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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