ArticleCell reports2022
Activation of Toll-like receptor 4 by Ebola virus-shed glycoprotein is direct and requires the internal fusion loop but not glycosylation.
Article in Cell reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- In Silico Modeling of Structural Compatibility and Alignment Between Viral Class I Fusion Cores and Human TLR4/MD-2.International journal of molecular sciences · 2026Article
- Review
- Interplay of TLR4 and SARS-CoV-2: Unveiling the Complex Mechanisms of Inflammation and Severity in COVID-19 Infections.Journal of inflammation research · 2024Review
- Activation of TLR4 by viral glycoproteins: A double-edged sword?Frontiers in microbiology · 2022Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Infection by the Ebola virus, a member of the Filoviridae family of RNA viruses, leads to acute viral hemorrhagic fever. End-stage Ebola virus disease is characterized by a cytokine storm that causes tissue damage, vascular disintegration, and multi-organ failure. Previous studies showed that a shed form of the viral spike glycoprotein (sGP1,2) drives this hyperinflammatory response by activating Toll-like receptor 4 (TLR4). Here, we find that glycosylation is not required for activation of TLR4 by sGP1,2 and identify the internal fusion loop (IFL) as essential for inflammatory signaling. sGP1,2 competes with lipid antagonists of TLR4, and the IFL interacts directly with TLR4 and co-receptor MD2. Together, these findings indicate that sGP1,2 activates TLR4 analogously to bacterial agonist lipopolysaccharide (LPS) by binding into a hydrophobic pocket in MD2 and promoting the formation of an active heterotetramer. This conclusion is supported by docking studies that predict binding sites for sGP1,2 on TLR4 and MD2.
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Registered trials
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