Evidence map›Paper›PMID 32948512›Full record

ArticleScience advances2020

Antibody-like proteins that capture and neutralize SARS-CoV-2.

T Kondo, Y Iwatani, K Matsuoka, T Fujino, S Umemoto, Y Yokomaku, K Ishizaki, S Kito, T Sezaki, G Hayashi and 1 more

Abstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Affinity Enhancement in Discrete Multivalent MegaMolecules.Chembiochem : a European journal of chemical biology · 2026
    Article
  3. Article
  4. Journal of the American Chemical Society · 2026
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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

11 authors.

T KondoDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.ORCID 0000-0003-2870-6956
Y IwataniDepartment of Infectious Diseases and Immunology, Clinical Research Center, National Hospital Organization Nagoya Medical Center, Nagoya, Japan.
K MatsuokaDepartment of Infectious Diseases and Immunology, Clinical Research Center, National Hospital Organization Nagoya Medical Center, Nagoya, Japan.ORCID 0000-0003-1217-3550
T FujinoDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.ORCID 0000-0002-1908-8757
S UmemotoDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.
Y YokomakuDepartment of Infectious Diseases and Immunology, Clinical Research Center, National Hospital Organization Nagoya Medical Center, Nagoya, Japan.
K IshizakiDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.ORCID 0000-0003-2880-0125
S KitoDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.ORCID 0000-0001-5223-7067
T SezakiDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.ORCID 0000-0003-3626-7885
G HayashiDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.
H MurakamiDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan. murah@chembio.nagoya-u.ac.jp.ORCID 0000-0003-2089-9263

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To combat severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) and any unknown emerging pathogens in the future, the development of a rapid and effective method to generate high-affinity antibodies or antibody-like proteins is of critical importance. We here report high-speed in vitro selection of multiple high-affinity antibody-like proteins against various targets including the SARS-CoV-2 spike protein. The sequences of monobodies against the SARS-CoV-2 spike protein were successfully procured within only 4 days. Furthermore, the obtained monobody efficiently captured SARS-CoV-2 particles from the nasal swab samples of patients and exhibited a high neutralizing activity against SARS-CoV-2 infection (half-maximal inhibitory concentration, 0.5 nanomolar). High-speed in vitro selection of antibody-like proteins is a promising method for rapid development of a detection method for, and of a neutralizing protein against, a virus responsible for an ongoing, and possibly a future, pandemic.

Indexed as

Amino Acid SequenceAngiotensin-Converting Enzyme 2Antibodies, ImmobilizedAntibodies, NeutralizingBetacoronavirusCell Surface Display TechniquesCoronavirus InfectionsCOVID-19DimerizationHumansKineticsPandemicsPeptidesPeptidyl-Dipeptidase APneumonia, ViralProtein DomainsACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, ImmobilizedAntibodies, NeutralizingPeptidesPeptidyl-Dipeptidase AProtein SubunitsRNA, ViralSingle-Domain AntibodiesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID32948512
PMCPMC7556756

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LicenceCC BY-NC
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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.