Evidence map›Paper›PMID 34874124›Full record

ArticleJournal of extracellular vesicles2021

Millisecond dynamic of SARS-CoV-2 spike and its interaction with ACE2 receptor and small extracellular vesicles.

Keesiang Lim, Goro Nishide, Takeshi Yoshida, Takahiro Watanabe-Nakayama, Akiko Kobayashi, Masaharu Hazawa, Rikinari Hanayama, Toshio Ando, Richard W Wong

Open access · goldAbstract read
In one paragraph

Article in Journal of extracellular vesicles, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.3field-weighted citation impact, top 6% of its field
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

34 citing papers in PubMed, 57 citations in OpenAlex.

  1. Human brain matters: Navigating the neuropathology of COVID-19.Brain pathology (Zurich, Switzerland) · 2026
    Review
  2. Article
  3. Switching Spike Plasticity Shapes ACE2 Engagement Across SARS-CoV-2 Variants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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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

9 authors at 2 institutions in 1 country.

Keesiang LimWPI-Nano Life Science Institute, Kanazawa University, Kanazawa, Ishikawa, Japan.
Goro NishideDivision of Nano Life Science in the Graduate School of Frontier Science Initiative, WISE Program for Nano-Precision Medicine, Science and Technology, Kanazawa University, Kanazawa, Ishikawa, Japan.
Takeshi YoshidaWPI-Nano Life Science Institute, Kanazawa University, Kanazawa, Ishikawa, Japan.
Takahiro Watanabe-NakayamaWPI-Nano Life Science Institute, Kanazawa University, Kanazawa, Ishikawa, Japan.
Akiko KobayashiCell-Bionomics Research Unit, Institute for Frontier Science Initiative (INFINITI), Kanazawa University, Kanazawa, Ishikawa, Japan.
Masaharu HazawaWPI-Nano Life Science Institute, Kanazawa University, Kanazawa, Ishikawa, Japan.
Rikinari HanayamaWPI-Nano Life Science Institute, Kanazawa University, Kanazawa, Ishikawa, Japan.
Toshio AndoWPI-Nano Life Science Institute, Kanazawa University, Kanazawa, Ishikawa, Japan.
Richard W WongWPI-Nano Life Science Institute, Kanazawa University, Kanazawa, Ishikawa, Japan.
Kanazawa University · JPLife Science Institute · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SARS-CoV-2 spike protein (S) binds to human angiotensin-converting enzyme 2 (hACE2), allowing virus to dock on cell membrane follow by viral entry. Here, we use high-speed atomic force microscopy (HS-AFM) for real-time visualization of S, and its interaction with hACE2 and small extracellular vesicles (sEVs). Results show conformational heterogeneity of S, flexibility of S stalk and receptor-binding domain (RBD), and pH/temperature-induced conformational change of S. S in an S-ACE2 complex appears as an all-RBD up conformation. The complex acquires a distinct topology upon acidification. S and S2 subunit demonstrate different membrane docking mechanisms on sEVs. S-hACE2 interaction facilitates S to dock on sEVs, implying the feasibility of ACE2-expressing sEVs for viral neutralization. In contrary, S2 subunit docks on lipid layer and enters sEV using its fusion peptide, mimicking the viral entry scenario. Altogether, our study provides a platform that is suitable for real-time visualization of various entry inhibitors, neutralizing antibodies, and sEV-based decoy in blocking viral entry. Teaser: Comprehensive observation of SARS-CoV-2 spike and its interaction with receptor ACE2 and sEV-based decoy in real time using HS-AFM.

Indexed as

Angiotensin-Converting Enzyme 2Extracellular VesiclesHumansHydrogen-Ion ConcentrationLipid BilayersMicroscopy, Atomic ForceProtein BindingProtein ConformationProtein DomainsProtein SubunitsSARS-CoV-2Spike Glycoprotein, CoronavirusTemperatureVirus InternalizationACE2 protein, humanAngiotensin-Converting Enzyme 2Lipid BilayersProtein SubunitsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2EVexosomesHigh-speed AFMSARS-CoV-2 spike

Identifiers

PMID34874124
PMCPMC8650025
OpenAlexW4200604504

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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 OpenQuestion graph.