ArticlemBio2025
β-Coronaviruses exploit ESCRT for virion assembly and egress.
Article in mBio, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Single-cell transcriptome profiling reveals herpesviral manipulation of host processes in spleen of gibel carp infected with a Cyvirus cyprinidallo2.PLoS pathogens · 2026Article
- Targeting the host factor HGS-viral membrane protein interaction in coronavirus infection.The Journal of clinical investigation · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
β-Coronaviruses assemble at the endoplasmic reticulum-to-Golgi compartment and exit cells through the lysosomal trafficking pathway. However, the molecular mechanisms of virion assembly and egress are largely unknown. Here, we report that β-coronaviruses recruit endosomal sorting complexes required for transport (ESCRTs) to facilitate virion assembly and egress. The viral proteins N and M interacted with ESCRT components TSG101 and VPS28, respectively. Electron microscopy analysis revealed that virion assembly was disrupted by TSG101 knockdown at an early stage and by VPS28 knockdown at a late stage. Knockdown of ESCRT components MVB12A and CHMP6 did not affect virion assembly but inhibited virion egress. Downregulation of these ESCRT factors or VPS4A, or treatment of cells with the TSG101 antagonist tenatoprazole significantly inhibited the production of the virion-like particles of β-coronaviruses and the replication of human coronavirus OC43. These findings indicate that β-coronaviruses exploit ESCRT for virion assembly and egress and suggest that the interaction interface between ESCRT and the viruses could be a target for the development of broad-spectrum anti-coronavirus therapeutics.IMPORTANCEβ-Coronaviruses have caused disastrous pandemics and may cause serious pandemics in the future. Virion assembly and egress are critical steps in the life cycle of coronaviruses. However, despite extensive studies in the past few years, the molecular mechanisms for virion assembly and egress are still largely unknown. Here we show that β-coronaviruses recruit ESCRT components TSG101 and VPS28 for virion assembly and that ESCRT components MVB12A and CHMP6 are required for virion egress. Treatment of cells with the TSG101 antagonist inhibited the assembly of multiple β-coronaviruses. These findings indicate that ESCRT participates in β-coronavirus assembly and egress and might be a potential target for the development of broad-spectrum anti-coronavirus therapeutics.
Indexed as
Identifiers
What OpenQuestion holds
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.