ArticleProceedings of the National Academy of Sciences of the United States of America2009
Alpha5beta1-integrin controls ebolavirus entry by regulating endosomal cathepsins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 91 citations in OpenAlex.
- The multifaceted roles of fibronectin in viral pathogenesis.Archives of virology · 2026Review
- The integrin protein ITGβ1 effectively suppresses porcine epidemic diarrhea virus replication through facilitating MDA5 oligomerization and subsequent activation of the type I interferon signaling pathway.Journal of virology · 2025Article
- Cathepsins in cellular entry of human pathogenic viruses.Journal of virology · 2025Review
- ITGB4/CD104 mediates zika virus attachment and infection.Nature communications · 2024Article
- N-Substituted Pyrrole-Based Heterocycles as Broad-Spectrum Filoviral Entry Inhibitors.Journal of medicinal chemistry · 2024Article
- Molecular insights into the Ebola virus life cycle.Nature microbiology · 2024Review
- A Receptor Integrin β1 Promotes Infection of Avian Metapneumovirus Subgroup C by Recognizing a Viral Fusion Protein RSD Motif.International journal of molecular sciences · 2024Article
- Contrasting effects of filamin A and B proteins in modulating filovirus entry.PLoS pathogens · 2023Article
- Review
- Targeting integrin pathways: mechanisms and advances in therapy.Signal transduction and targeted therapy · 2023Review
- Pseudotyped Viruses for Marburgvirus and Ebolavirus.Advances in experimental medicine and biology · 2023Article
- Influenza A Virus Uses PSMA2 for Downregulation of the NRF2-Mediated Oxidative Stress Response.Journal of virology · 2022Article
- Integrins as Therapeutic Targets for SARS-CoV-2.Frontiers in cellular and infection microbiology · 2022Article
- Emerging therapeutic opportunities for integrin inhibitors.Nature reviews. Drug discovery · 2022Review
- αVβ3 Integrin Expression Is Essential for Replication of Mosquito and Tick-Borne Flaviviruses in Murine Fibroblast Cells.Viruses · 2021Article
- Advancing cell instructive biomaterials through increased understanding of cell receptor spacing and material surface functionalization.Regenerative engineering and translational medicine · 2021Article
- Immunization and Drug Metabolizing Enzymes: Focus on Hepatic Cytochrome P450 3A.Expert review of vaccines · 2021Article
- Ins and Outs of Reovirus: Vesicular Trafficking in Viral Entry and Egress.Trends in microbiology · 2021Review
- Hypothetical targets and plausible drugs of coronavirus infection caused by SARS-CoV-2.Transboundary and emerging diseases · 2021Review
- RGD-binding integrins and TGF-β in SARS-CoV-2 infections - novel targets to treat COVID-19 patients?Clinical & translational immunology · 2021Review
2 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Integrins are involved in the binding and internalization of both enveloped and nonenveloped viruses. By using 3 distinct cell systems-CHO cells lacking expression of alpha(5)beta(1)-integrin, HeLa cells treated with siRNA to alpha(5)-integrin, and mouse beta(1)-integrin knockout fibroblasts, we show that alpha(5)beta(1)-integrin is required for efficient infection by pseudovirions bearing the ebolavirus glycoprotein (GP). These integrins are necessary for viral entry but not for binding or internalization. Given the need for endosomal cathepsins B and L (CatB and CatL) to prime GPs for fusion, we investigated the status of CatB and CatL in integrin-positive and integrin-negative cell lines. Alpha(5)beta(1)-Integrin-deficient cells lacked the double-chain (DC) forms of CatB and CatL, and this correlated with decreased CatL activity in integrin-negative CHO cells. These data indicate that alpha(5)beta(1)-integrin-negative cells may be refractory to infection by GP pseudovirions because they lack the necessary priming machinery (the double-chain forms of CatB and CatL). In support of this model, we show that GP pseudovirions that have been preprimed in vitro to generate the 19-kDa form of GP overcome the requirement for alpha(5)beta(1)-integrin for infection. These results provide further support for the requirement for endosomal cathepsins for ebolavirus infection, identify the DC forms of these cathepsins as previously unrecognized factors that contribute to cell tropism of this virus, and reveal a previously undescribed role for integrins during viral entry as regulators of endosomal cathepsins, which are required to prime the entry proteins of ebolavirus and other pathogenic viruses.
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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.