Evidence map›Paper›PMID 39611845›Full record

ArticlemBio2025

Coatomer complex I is required for the transport of SARS-CoV-2 progeny virions from the endoplasmic reticulum-Golgi intermediate compartment.

Ai Hirabayashi, Yukiko Muramoto, Toru Takenaga, Yugo Tsunoda, Mayumi Wakazaki, Mayuko Sato, Yoko Fujita-Fujiharu, Norimichi Nomura, Koji Yamauchi, Chiho Onishi and 3 more

Abstract read
In one paragraph

Article in mBio, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Virus infection and vesicle trafficking.Frontiers in immunology · 2025
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Ai HirabayashiLaboratory of Ultrastructural Virology, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Kyoto Prefecture, Japan.
Yukiko MuramotoLaboratory of Ultrastructural Virology, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Kyoto Prefecture, Japan.
Toru TakenagaLaboratory of Ultrastructural Virology, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Kyoto Prefecture, Japan.
Yugo TsunodaLaboratory of Ultrastructural Virology, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Kyoto Prefecture, Japan.
Mayumi WakazakiRIKEN Center for Sustainable Resource Science, Yokohama, Kanagawa Prefecture, Japan.
Mayuko SatoRIKEN Center for Sustainable Resource Science, Yokohama, Kanagawa Prefecture, Japan.
Yoko Fujita-FujiharuLaboratory of Ultrastructural Virology, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Kyoto Prefecture, Japan.ORCID 0000-0002-2411-5473
Norimichi NomuraDepartment of Cell Biology, Graduate School of Medicine, Kyoto University, , Kyoto, Kyoto Prefecture, Japan.ORCID 0000-0002-6330-2239
Koji YamauchiLaboratory of Ultrastructural Virology, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Kyoto Prefecture, Japan.
Chiho OnishiLaboratory of Ultrastructural Virology, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Kyoto Prefecture, Japan.
Masahiro NakanoLaboratory of Ultrastructural Virology, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Kyoto Prefecture, Japan.ORCID 0000-0003-4247-9008
Kiminori ToyookaRIKEN Center for Sustainable Resource Science, Yokohama, Kanagawa Prefecture, Japan.
Takeshi NodaLaboratory of Ultrastructural Virology, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Kyoto Prefecture, Japan.ORCID 0000-0002-0658-4663

Funding

Japan Agency for Medical Research and Development (AMED) 24fk0108694h0001,JP23fm0208101,22KK0115Japan Agency for Medical Research and Development (AMED) JP22ama121007MEXT | Japan Science and Technology Agency (JST) JPMJCR20HAMEXT | Japan Society for the Promotion of Science (JSPS) JPJSCCA20240006,JPJSCCA20190008,22K19431Takeda Science Foundation (TSF)
6 · The paper itself

Abstract

SARS-CoV-2 undergoes budding within the lumen of the endoplasmic reticulum-Golgi intermediate compartment (ERGIC), and the progeny virions are delivered to the cell surface via vesicular transport. However, the molecular mechanisms remain poorly understood. Using three-dimensional electron microscopic analysis, such as array tomography and electron tomography, we found that virion-transporting vesicles possessed protein coats on their membrane and demonstrated that the protein coat was coatomer complex I (COPI). During the later stages of SARS-CoV-2 infection, we observed a notable alteration in the distribution of COPI and ERGIC throughout the cytoplasm, suggesting their potential involvement in virus replication. Depletion of COPB2, a key component of COPI, led to the confinement of SARS-CoV-2 progeny virions within the ERGIC at the perinuclear region. While the expression levels of viral proteins within cells were comparable, this depletion significantly reduced the efficiency of virion release, leading to the significant reduction of viral replication. Hence, our findings suggest COPI as a critical player in facilitating the transport of SARS-CoV-2 progeny virions from the ERGIC. Thus, COPI could be a promising target for the development of antivirals against SARS-CoV-2. IMPORTANCE: SARS-CoV-2 virions are synthesized within the ERGIC and are transported to the cell surface via vesicular transport for release. However, the precise mechanisms remain unclear. Through various electron microscopic techniques, we identified the presence of COPI on virion-transporting vesicles. Alterations in the distribution of COPI and ERGIC in SARS-CoV-2 infected cells are evident, suggesting their involvement in virus replication. When COPB2, a component of COPI, is depleted, progeny virions become trapped within the ERGIC, leading to a reduction in the efficiency of virion release. These findings highlight COPI's crucial role in mediating SARS-CoV-2 vesicular transport from the ERGIC and suggest it as a potential antiviral target.

Indexed as

Coat Protein Complex IEndoplasmic ReticulumGolgi ApparatusSARS-CoV-2VirionVirus ReplicationAnimalsBiological TransportChlorocebus aethiopsCOVID-19Electron Microscope TomographyHumansVero CellsVirus ReleaseCoat Protein Complex ICOPISARS-CoV-2vesicular transport

Identifiers

PMID39611845
PMCPMC11708035

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 Socratic graph.