ArticleNature communications2024
Endosomal fusion of pH-dependent enveloped viruses requires ion channel TRPM7.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Visualization of Endosomal Escape of Intracellularly Delivered Protein With Unexpected Photochemical Internalization of Trypan Blue.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Chitosan-EDTA-cellulose functionalized with β-cyclodextrin as a pH-sensitive bio-based nanocarrier for curcumin drug delivery.Scientific reports · 2026Article
- Article
- Review
- Targeting virus-interacting host ion channels as a novel antiviral strategy.Acta pharmacologica Sinica · 2026Review
- Membrane Fusion-Inspired Nanomaterials: Emerging Strategies for Infectious Disease and Cancer Diagnostics.Advanced healthcare materials · 2026Review
- P-glycoprotein exofection between fetal and maternal cells as a mechanism of intercellular material transfer at the feto maternal interface.bioRxiv : the preprint server for biology · 2026Article
- Bovine coronavirus enters HRT-18 cells via membrane fusion and clathrin-mediated endocytosis in a low pH-, dynamin-, cholesterol-, microtubule-, Rab7-, and Rab11-dependent manner.Journal of virology · 2025Article
- Adaptor protein complex 1 gamma 1 subunit is an important host factor involved in both Zika virus and dengue virus infections.Virologica Sinica · 2025Article
- Revealing hidden protonated conformational states in RNA dynamic ensembles.Nucleic acids research · 2025Article
- Inter-Organellar CaCells · 2025Review
- Transcriptional Analysis ofInternational journal of molecular sciences · 2025Article
- Metabolic characteristics in orthoflaviviral infections: unveiling pathogenic mechanisms and therapeutic targets.Virology journal · 2025Review
Corrections and comments
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Authors and funding
21 authors.
Funding
Abstract
The majority of viruses classified as pandemic threats are enveloped viruses which enter the cell through receptor-mediated endocytosis and take advantage of endosomal acidification to activate their fusion machinery. Here we report that the endosomal fusion of low pH-requiring viruses is highly dependent on TRPM7, a widely expressed TRP channel that is located on the plasma membrane and in intracellular vesicles. Using several viral infection systems expressing the envelope glycoproteins of various viruses, we find that loss of TRPM7 protects cells from infection by Lassa, LCMV, Ebola, Influenza, MERS, SARS-CoV-1, and SARS-CoV-2. TRPM7 ion channel activity is intrinsically necessary to acidify virus-laden endosomes but is expendable for several other endosomal acidification pathways. We propose a model wherein TRPM7 ion channel activity provides a countercurrent of cations from endosomal lumen to cytosol necessary to sustain the pumping of protons into these virus-laden endosomes. This study demonstrates the possibility of developing a broad-spectrum, TRPM7-targeting antiviral drug to subvert the endosomal fusion of low pH-dependent enveloped viruses.
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