Evidence map›Paper›PMID 35891441›Full record

ArticleViruses2022

Characterization and Utilization of Disulfide-Bonded SARS-CoV-2 Receptor Binding Domain of Spike Protein Synthesized by Wheat Germ Cell-Free Production System.

Yutaro Yamaoka, Sundararaj Stanleyraj Jeremiah, Rikako Funabashi, Kei Miyakawa, Takeshi Morita, Yusaku Mihana, Hideaki Kato, Akihide Ryo

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
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  11. Solid-Phase Cell-Free Protein Synthesis and Its Applications in Biotechnology.Advances in biochemical engineering/biotechnology · 2023
    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

8 authors at 3 institutions in 1 country.

Yutaro YamaokaDepartment of Microbiology, Yokohama City University Graduate School of Medicine, Yokohama 236-0004, Japan.
Sundararaj Stanleyraj JeremiahDepartment of Microbiology, Yokohama City University Graduate School of Medicine, Yokohama 236-0004, Japan.
Rikako FunabashiDepartment of Microbiology, Yokohama City University Graduate School of Medicine, Yokohama 236-0004, Japan.
Kei MiyakawaDepartment of Microbiology, Yokohama City University Graduate School of Medicine, Yokohama 236-0004, Japan.
Takeshi MoritaDepartment of Microbiology, Yokohama City University Graduate School of Medicine, Yokohama 236-0004, Japan.ORCID 0000-0001-5109-2003
Yusaku MihanaDepartment of Microbiology, Yokohama City University Graduate School of Medicine, Yokohama 236-0004, Japan.
Hideaki KatoInfection Prevention and Control Department, Yokohama City University Hospital, Yokohama 236-0004, Japan.ORCID 0000-0002-7853-5721
Akihide RyoDepartment of Microbiology, Yokohama City University Graduate School of Medicine, Yokohama 236-0004, Japan.
Yokohama City University · JPKanto Chemical (Japan) · JPYokohama City University Hospital · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The spike protein (SP) of SARS-CoV-2 is an important target for COVID-19 therapeutics and vaccines as it binds to the ACE2 receptor and enables viral infection. Rapid production and functional characterization of properly folded SP is of the utmost importance for studying the immunogenicity and receptor-binding activity of this protein considering the emergence of highly infectious viral variants. In this study, we attempted to express the receptor-binding region (RBD) of SARS-CoV-2 SP containing disulfide bonds using the wheat germ cell-free protein synthesis system. By adding protein disulfide isomerase (PDI) and endoplasmic reticulum oxidase (ERO1α) to the translational reaction mixture, we succeeded in synthesizing a functionally intact RBD protein that can interact with ACE2. Using this RBD protein, we have developed a high-throughput AlphaScreen assay to evaluate the RBD-ACE2 interaction, which can be applied for drug screening and mutation analysis. Thus, our method sheds new light on the structural and functional properties of SARS-CoV-2 SP and has the potential to contribute to the development of new COVID-19 therapeutics.

Indexed as

COVID-19SARS-CoV-2Angiotensin-Converting Enzyme 2DisulfidesPeptidyl-Dipeptidase AProtein BindingSpike Glycoprotein, CoronavirusTriticumAngiotensin-Converting Enzyme 2DisulfidesPeptidyl-Dipeptidase ASpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2cell-free protein synthesisCOVID-19disulfide bonddrug screeningRBDSARS-CoV-2

Identifiers

PMID35891441
PMCPMC9321213
OpenAlexW4283816888

What OpenQuestion 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 OpenQuestion graph.