ArticlePLoS pathogens2018
Ebola virus requires a host scramblase for externalization of phosphatidylserine on the surface of viral particles.
Article in PLoS pathogens, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 62 citations in OpenAlex.
- Multi-omics dissection of metabolic hijacking: Infectious bronchitis virus orchestrates lipid-centric replication through PPAR-TGF-β crosstalk.Virulence · 2026Article
- TAM receptor tyrosine kinases as potential mediators of the non-lytic spread of non-enveloped viruses.Biochemical Society transactions · 2026Review
- Targeting envelope lipids with 2,6‑di‑Journal of virology · 2025Article
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- Visualizing the Internalization of Marburg Viruslike Particles into Living Cells.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Expression, purification and characterization of phosphatidylserine-targeting antibodies for biochemical and therapeutic applications.Methods in cell biology · 2025Article
- TMEM16 and OSCA/TMEM63 proteins share a conserved potential to permeate ions and phospholipids.eLife · 2024Article
- TMEM16 and OSCA/TMEM63 proteins share a conserved potential to permeate ions and phospholipids.bioRxiv : the preprint server for biology · 2024Article
- Marburg virus exploits the Rab11-mediated endocytic pathway in viral-particle production.Microbiology spectrum · 2024Article
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- Molecular insights into the Ebola virus life cycle.Nature microbiology · 2024Review
- Minor changes in electrostatics robustly increase VP40 membrane binding, assembly, and budding of Ebola virus matrix protein derived virus-like particles.bioRxiv : the preprint server for biology · 2024Article
- Navigating the Complex Landscape of Ebola Infection Treatment: A Review of Emerging Pharmacological Approaches.Infectious diseases and therapy · 2024Review
- SARS-CoV-2 Syncytium under the Radar: Molecular Insights of the Spike-Induced Syncytia and Potential Strategies to Limit SARS-CoV-2 Replication.Journal of clinical medicine · 2023Review
- Chikungunya virus entry and infectivity is primarily facilitated through cell line dependent attachment factors in mammalian and mosquito cells.Frontiers in cell and developmental biology · 2023Article
- The Art of Viral Membrane Fusion and Penetration.Sub-cellular biochemistry · 2023Article
- Phosphatidylserine clustering by the Ebola virus matrix protein is a critical step in viral budding.EMBO reports · 2022Article
- RNA Viruses, Pregnancy and Vaccination: Emerging Lessons from COVID-19 and Ebola Virus Disease.Pathogens (Basel, Switzerland) · 2022Review
- TIM-1 Augments Cellular Entry of Ebola Virus Species and Mutants, Which Is Blocked by Recombinant TIM-1 Protein.Microbiology spectrum · 2022Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell surface receptors for phosphatidylserine contribute to the entry of Ebola virus (EBOV) particles, indicating that the presence of phosphatidylserine in the envelope of EBOV is important for the internalization of EBOV particles. Phosphatidylserine is typically distributed in the inner layer of the plasma membrane in normal cells. Progeny virions bud from the plasma membrane of infected cells, suggesting that phosphatidylserine is likely flipped to the outer leaflet of the plasma membrane in infected cells for EBOV virions to acquire it. Currently, the intracellular dynamics of phosphatidylserine during EBOV infection are poorly understood. Here, we explored the role of XK-related protein (Xkr) 8, which is a scramblase responsible for exposure of phosphatidylserine in the plasma membrane of apoptotic cells, to understand its significance in phosphatidylserine-dependent entry of EBOV. We found that Xkr8 and transiently expressed EBOV glycoprotein GP often co-localized in intracellular vesicles and the plasma membrane. We also found that co-expression of GP and viral major matrix protein VP40 promoted incorporation of Xkr8 into ebolavirus-like particles (VLPs) and exposure of phosphatidylserine on their surface, although only a limited amount of phosphatidylserine was exposed on the surface of the cells expressing GP and/or VP40. Downregulating Xkr8 or blocking caspase-mediated Xkr8 activation did not affect VLP production, but they reduced the amount of phosphatidylserine on the VLPs and their uptake in recipient cells. Taken together, our findings indicate that Xkr8 is trafficked to budding sites via GP-containing vesicles, is incorporated into VLPs, and then promote the entry of the released EBOV to cells in a phosphatidylserine-dependent manner.
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