ArticleCells2021
The Phosphatidylserine Receptor TIM-1 Enhances Authentic Chikungunya Virus Cell Entry.
Article in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 48 citations in OpenAlex.
- Research progress on the role of host factors in Chikungunya virus infection and intervention strategies.Virulence · 2026Review
- TIM-1 promotes infection with mosquito cell-derived alphaviruses through virion-associated phospholipids.Emerging microbes & infections · 2026Article
- Outer membrane vesicles hijack TIM-1 for cellular uptake.PLoS pathogens · 2026Article
- AGPAT1 is a novel Chikungunya virus receptor on human cells.Journal of virology · 2026Article
- Exploring the potential of oxymatrine in preventing CHIKV-induced acute kidney injury based on multi-dimensional computational analysis andFrontiers in microbiology · 2026Article
- Viral Vertical Transmission through the Placenta: The Potential of Natural Products as Therapeutic and Prophylactic Antiviral Agents.Current topics in medicinal chemistry · 2026Review
- Article
- Review
- Chikungunya virus and other emerging arthritogenic alphaviruses.Nature reviews. Microbiology · 2025Review
- Determinants of human versus mosquito cell entry by the Chikungunya virus envelope proteins.bioRxiv : the preprint server for biology · 2025Article
- Review
- Infectomics of Chikungunya Virus: Roles Played by Host Factors.The American journal of tropical medicine and hygiene · 2025Review
- Exploring the antiviral potential of shikimic acid against Chikungunya virus through network pharmacology, molecular docking, andFrontiers in veterinary science · 2025Article
- Pathogenicity and virulence of chikungunya virus.Virulence · 2024Review
- Insights into mosquito-borne arbovirus receptors.Cell insight · 2024Review
- Nano-Biomechanical Investigation of Phosphatidylserine-Mediated Ebola Viral Attachment via Human Gas6 and Axl.Viruses · 2024Article
- Chikungunya virus release is reduced by TIM-1 receptors through binding of envelope phosphatidylserine.Journal of virology · 2024Article
- Glucosylceramide in bunyavirus particles is essential for virus binding to host cells.Cellular and molecular life sciences : CMLS · 2024Article
- Chikungunya Virus Release is Reduced by TIM-1 Receptors Through Binding of Envelope Phosphatidylserine.bioRxiv : the preprint server for biology · 2024Article
- Antiviral Activity of Anthranilamide Peptidomimetics against Herpes Simplex Virus 1 and a Coronavirus.Antibiotics (Basel, Switzerland) · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Chikungunya virus (CHIKV) is a re-emerging, mosquito-transmitted, enveloped positive stranded RNA virus. Chikungunya fever is characterized by acute and chronic debilitating arthritis. Although multiple host factors have been shown to enhance CHIKV infection, the molecular mechanisms of cell entry and entry factors remain poorly understood. The phosphatidylserine-dependent receptors, T-cell immunoglobulin and mucin domain 1 (TIM-1) and Axl receptor tyrosine kinase (Axl), are transmembrane proteins that can serve as entry factors for enveloped viruses. Previous studies used pseudoviruses to delineate the role of TIM-1 and Axl in CHIKV entry. Conversely, here, we use the authentic CHIKV and cells ectopically expressing TIM-1 or Axl and demonstrate a role for TIM-1 in CHIKV infection. To further characterize TIM-1-dependent CHIKV infection, we generated cells expressing domain mutants of TIM-1. We show that point mutations in the phosphatidylserine binding site of TIM-1 lead to reduced cell binding, entry, and infection of CHIKV. Ectopic expression of TIM-1 renders immortalized keratinocytes permissive to CHIKV, whereas silencing of endogenously expressed TIM-1 in human hepatoma cells reduces CHIKV infection. Altogether, our findings indicate that, unlike Axl, TIM-1 readily promotes the productive entry of authentic CHIKV into target cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.