ArticleJournal of virology2007
A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane.
Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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
52 citing papers in PubMed, 82 citations in OpenAlex.
- Remodeling of the cellular membrane architecture in response to BK polyomavirus infection.Virology journal · 2026Review
- Temporal gating of nuclear import: How Merkel cell polyomavirus exploits the cell cycle for nuclear entry.PLoS pathogens · 2025Article
- From the Cytoplasm into the Nucleus-Hepatitis B Virus Travel and Genome Repair.Microorganisms · 2025Review
- Reticulophagy and viral infection.Autophagy · 2025Review
- BK Polyomavirus Infection of Bladder Microvascular Endothelial Cells Leads to the Activation of the cGAS-STING Pathway.Journal of medical virology · 2024Article
- The atlastin ER morphogenic proteins promote formation of a membrane penetration site during non-enveloped virus entry.Journal of virology · 2023Article
- Nuclear Cytoskeleton in Virus Infection.International journal of molecular sciences · 2022Review
- Spike S1 domain interactome in non-pulmonary systems: A role beyond the receptor recognition.Frontiers in molecular biosciences · 2022Article
- Lunapark-dependent formation of a virus-induced ER exit site contains multi-tubular ER junctions that promote viral ER-to-cytosol escape.Cell reports · 2021Article
- Review
- Sending mixed signals: polyomavirus entry and trafficking.Current opinion in virology · 2021Review
- ER functions are exploited by viruses to support distinct stages of their life cycle.Biochemical Society transactions · 2020Review
- Ubqln4 Facilitates Endoplasmic Reticulum-to-Cytosol Escape of a Nonenveloped Virus during Infection.Journal of virology · 2020Article
- SV40 Hijacks Cellular Transport, Membrane Penetration, and Disassembly Machineries to Promote Infection.Viruses · 2019Review
- Bag2 Is a Component of a Cytosolic Extraction Machinery That Promotes Membrane Penetration of a Nonenveloped Virus.Journal of virology · 2018Article
- Dynein Engages and Disassembles Cytosol-Localized Simian Virus 40 To Promote Infection.Journal of virology · 2018Article
- Article
- Exploiting the kinesin-1 molecular motor to generate a virus membrane penetration site.Nature communications · 2017Article
- EMC1-dependent stabilization drives membrane penetration of a partially destabilized non-enveloped virus.eLife · 2016Article
- Opportunistic intruders: how viruses orchestrate ER functions to infect cells.Nature reviews. Microbiology · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The nonenveloped polyomavirus (Py) traffics from the plasma membrane to the endoplasmic reticulum (ER), where it penetrates the ER membrane, allowing the viral genome to reach the nucleus to cause infection. The mechanism of membrane penetration for Py, and for other nonenveloped viruses, remains poorly characterized. We showed previously that the ER chaperone ERp29 alters the conformation of Py coat protein VP1, enabling the virus to interact with membranes. Here, we developed a membrane perforation assay and showed that the ERp29-activated Py perforates the physiologically relevant ER membrane, an event that likely initiates viral penetration. Biochemical analysis revealed that the internal protein VP2 is exposed in the activated viral particle. Accordingly, we demonstrate that VP2 binds to, integrates into, and perforates the ER membrane; the other internal protein, VP3, binds to and integrates into the ER membrane but is not sufficient for perforation. Our data thus link the activity of a cellular factor on a nonenveloped virus to the membrane perforation event and identify a viral component that mediates this process.
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.