Evidence map›Paper›PMID 38961055›Full record

ArticleNature communications2024

Recreating the biological steps of viral infection on a cell-free bioelectronic platform to profile viral variants of concern.

Zhongmou Chao, Ekaterina Selivanovitch, Konstantinos Kallitsis, Zixuan Lu, Ambika Pachaury, Róisín Owens, Susan Daniel

Abstract read
In one paragraph

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 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Emerging Designs and Applications for Biomembrane Biosensors.Annual review of analytical chemistry (Palo Alto, Calif.) · 2024
    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

7 authors.

Zhongmou Chao *Robert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, 124 Olin Hall, Ithaca, NY, 14853, USA.ORCID 0000-0002-9882-4440
Ekaterina Selivanovitch *Robert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, 124 Olin Hall, Ithaca, NY, 14853, USA.ORCID 0000-0001-7140-7631
Konstantinos KallitsisDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Philippa Fawcett Dr., Cambridge, CB3 0AS, UK.ORCID 0000-0001-5480-4483
Zixuan LuDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Philippa Fawcett Dr., Cambridge, CB3 0AS, UK.ORCID 0000-0002-3689-4283
Ambika PachauryRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, 124 Olin Hall, Ithaca, NY, 14853, USA.
Róisín OwensDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Philippa Fawcett Dr., Cambridge, CB3 0AS, UK.ORCID 0000-0001-7856-2108
Susan DanielRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, 124 Olin Hall, Ithaca, NY, 14853, USA. sd386@cornell.edu.ORCID 0000-0001-7773-0835

Funding

Designing addressable proteoliposomes by using viral transmembrane proteins and biomimetic cell-free synthesis techniques.F32AI183691 · NIAID · CORNELL UNIVERSITY · PI Ekaterina Selivanovitch · 2024 to 2026
$234k
NIAID NIH HHS F32 AI183691
6 · The paper itself

Abstract

Viral mutations frequently outpace technologies used to detect harmful variants. Given the continual emergence of SARS-CoV-2 variants, platforms that can identify the presence of a virus and its propensity for infection are needed. Our electronic biomembrane sensing platform recreates distinct SARS-CoV-2 host cell entry pathways and reports the progression of entry as electrical signals. We focus on two necessary entry processes mediated by the viral Spike protein: virus binding and membrane fusion, which can be distinguished electrically. We find that closely related variants of concern exhibit distinct fusion signatures that correlate with trends in cell-based infectivity assays, allowing us to report quantitative differences in their fusion characteristics and hence their infectivity potentials. We use SARS-CoV-2 as our prototype, but we anticipate that this platform can extend to other enveloped viruses and cell lines to quantifiably assess virus entry.

Indexed as

COVID-19SARS-CoV-2Spike Glycoprotein, CoronavirusVirus InternalizationCell-Free SystemHumansMembrane FusionMutationVirus AttachmentSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID38961055
PMCPMC11222515

What OpenQuestion holds

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LicenceCC BY
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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.