MassIVE MSV000093669

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A protein-proximity screen reveals that Ebola virus co-opts the mRNA decapping complex through the scaffold protein EDC4

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Description

Understanding the molecular interactions of host cells with Ebola virus (EBOV) is integral for further therapeutic development of antivirals. We performed a proximity-dependent protein interaction screen for six of seven EBOV proteins to characterize the EBOV-host interactome. Using network analysis, putative EBOV interacting proteins were mapped to a human protein interactome. We overlayed viral protein interactions onto the host network. Within this map, several known EBOV-host protein interactions were identified, as well as several cell processes, such as RNA processing, previously implicated in EBOV replication. Furthermore, this interactome revealed novel interactions between EBOV proteins and host proteins arranged in functional complexes. As proof of this concept, we characterized the interaction between EBOV VP35 and the mRNA decapping complex, which regulates mRNA turnover in host cells. Our protein-protein interaction data demonstrate that VP35 engages multiple components of this complex by binding binds the scaffold protein EDC4. Inhibiting expression of mRNA decapping complex components EDC4, EDC3, or DCP2 inhibited viral replication by reducing early viral RNA synthesis. Our approach examining EBOV-host protein interactions in conjunction with network analysis reveals how EBOV interacts with entire cellular machines as opposed to singular cell proteins to promote its replication. [doi:10.25345/C55D8NR4W] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Ebola virus, proximity labeling, mRNA decaping complex, Scafold Protein

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Principal Investigators:
(in alphabetical order) 		Douglas J. LaCount, Medicinal Chemistry and Molecular Pharmacology, Purdue University, United States
Submitting User: uma_aryal
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