ArticleThe EMBO journal2021
Non-canonical proline-tyrosine interactions with multiple host proteins regulate Ebola virus infection.
Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Infection-sensing minigenome as a novel therapeutic approach against Ebola virus.Molecular therapy. Nucleic acids · 2025Article
- Molecular insights into nucleocapsid assembly and transport in Marburg and Ebola viruses.mBio · 2025Article
- State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025Review
- Hippo signaling pathway regulates Ebola virus transcription and egress.Nature communications · 2024Article
- Molecular insights into the Ebola virus life cycle.Nature microbiology · 2024Review
- Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets.Nature communications · 2023Article
- NAT10-mediated RNA acetylation enhances HNRNPUL1 mRNA stability to contribute cervical cancer progression.International journal of medical sciences · 2023Article
- Article
- Evidence for Viral mRNA Export from Ebola Virus Inclusion Bodies by the Nuclear RNA Export Factor NXF1.Journal of virology · 2022Article
- Domain-specific biochemical and serological characterization of SARS-CoV-2 nucleocapsid protein.STAR protocols · 2021Article
- Non-canonical proline-tyrosine interactions with multiple host proteins regulate Ebola virus infection.The EMBO journal · 2021Article
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Authors and funding
17 authors at 6 institutions in 2 countries.
Funding
Abstract
The Ebola virus VP30 protein interacts with the viral nucleoprotein and with host protein RBBP6 via PPxPxY motifs that adopt non-canonical orientations, as compared to other proline-rich motifs. An affinity tag-purification mass spectrometry approach identified additional PPxPxY-containing host proteins hnRNP L, hnRNPUL1, and PEG10, as VP30 interactors. hnRNP L and PEG10, like RBBP6, inhibit viral RNA synthesis and EBOV infection, whereas hnRNPUL1 enhances. RBBP6 and hnRNP L modulate VP30 phosphorylation, increase viral transcription, and exert additive effects on viral RNA synthesis. PEG10 has more modest inhibitory effects on EBOV replication. hnRNPUL1 positively affects viral RNA synthesis but in a VP30-independent manner. Binding studies demonstrate variable capacity of the PPxPxY motifs from these proteins to bind VP30, define PxPPPPxY as an optimal binding motif, and identify the fifth proline and the tyrosine as most critical for interaction. Competition binding and hydrogen-deuterium exchange mass spectrometry studies demonstrate that each protein binds a similar interface on VP30. VP30 therefore presents a novel proline recognition domain that is targeted by multiple host proteins to modulate viral transcription.
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