Evidence map›Paper›PMID 36827795›Full record

ArticleBiosensors & bioelectronics2023

The SpACE-CCM: A facile and versatile cell culture medium-based biosensor for detection of SARS-CoV-2 spike-ACE2 interaction.

Youngwook Ham, Nam-Chul Cho, Daeyong Kim, Jung-Hee Kim, Min Ju Jo, Min Seon Jeong, Bo-Yeong Pak, Sanghyeok Lee, Mi-Kyung Lee, Seung-Wook Chi and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Biosensors & bioelectronics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.6field-weighted citation impact, top 37% 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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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 at 3 institutions in 1 country.

Youngwook HamNucleic Acid Therapeutics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Cheongju, Chungbuk, 28116, Republic of Korea; Department of Biomolecular Science, KRIBB School of Bioscience, Korea University of Science and Technology (KUST), Daejeon, 34113, Republic of Korea.
Nam-Chul ChoKorea Chemical Bank, Korea Research Institute of Chemical Technology (KRICT), Daejeon, 34114, Republic of Korea.
Daeyong KimNucleic Acid Therapeutics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Cheongju, Chungbuk, 28116, Republic of Korea; Department of Biomolecular Science, KRIBB School of Bioscience, Korea University of Science and Technology (KUST), Daejeon, 34113, Republic of Korea.
Jung-Hee KimAM Science Corp., Gyeonggi, 12902, Republic of Korea.
Min Ju JoNucleic Acid Therapeutics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Cheongju, Chungbuk, 28116, Republic of Korea; College of Pharmacy, Chungbuk National University, Chungbuk, 28644, Republic of Korea.
Min Seon JeongNucleic Acid Therapeutics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Cheongju, Chungbuk, 28116, Republic of Korea; Department of Biomolecular Science, KRIBB School of Bioscience, Korea University of Science and Technology (KUST), Daejeon, 34113, Republic of Korea.
Bo-Yeong PakAM Science Corp., Gyeonggi, 12902, Republic of Korea.
Sanghyeok LeeAM Science Corp., Gyeonggi, 12902, Republic of Korea.
Mi-Kyung LeeDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, Republic of Korea; Critical Diseases Diagnostics Convergence Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, Republic of Korea; Department of Proteome Structural Biology, KRIBB School of Bioscience, Korea University of Science and Technology (KUST), Daejeon, 34113, Republic of Korea.
Seung-Wook ChiDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, Republic of Korea; Department of Proteome Structural Biology, KRIBB School of Bioscience, Korea University of Science and Technology (KUST), Daejeon, 34113, Republic of Korea.
Tae-Don KimImmunotherapy Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, Republic of Korea; Department of Functional Genomics, KRIBB School of Bioscience, Korea University of Science and Technology (KUST), Daejeon, 34113, Republic of Korea.
Nak Cheol JeongAM Science Corp., Gyeonggi, 12902, Republic of Korea.
Sungchan ChoNucleic Acid Therapeutics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Cheongju, Chungbuk, 28116, Republic of Korea; Department of Biomolecular Science, KRIBB School of Bioscience, Korea University of Science and Technology (KUST), Daejeon, 34113, Republic of Korea. Electronic address: sungchan@kribb.re.kr.
Korea Research Institute of Bioscience and Biotechnology · KRChungbuk National University · KRKorea Research Institute of Chemical Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The COVID-19 pandemic is an ongoing global public health threat. COVID-19 is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection, and binding of the SARS-CoV-2 spike to its receptor, angiotensin-converting enzyme 2 (ACE2), on host cells is critical for viral infection. Here, we developed a luminescent biosensor that readily detects interactions of the spike receptor-binding domain (RBD) and ACE2 in cell culture medium ('SpACE-CCM'), which was based on bimolecular complementation of the split nanoluciferase-fused spike RBD and ectodomain of ACE2 and further engineered to be efficiently secreted from cells by adding a heterologous secretory signal peptide (SSP). Screening of various SSPs identified 'interferon-α+alanine-aspartate' as the SSP that induced the highest activity. The SpACE-CCM biosensor was validated by observing a marked reduction of the activity caused by interaction-defective mutations or in the presence of neutralizing antibodies, recombinant decoy proteins, or peptides. Importantly, the SpACE-CCM biosensor responded well in assay-validating conditions compared with conventional cell lysate-based NanoLuc Binary Technology, indicating its advantage. We further demonstrated the biosensor's versatility by quantitatively detecting neutralizing activity in blood samples from COVID-19 patients and vaccinated individuals, discovering a small molecule interfering with the spike RBD-ACE2 interaction through high-throughput screening, and assessing the cross-reactivity of neutralizing antibodies against SARS-CoV-2 variants. Because the SpACE-CCM is a facile and rapid one-step reaction biosensor that aptly recapitulates the native spike-ACE2 interaction, it would be advantageous in many experimental and clinical applications associated with this interaction.

Indexed as

Biosensing TechniquesCOVID-19Angiotensin-Converting Enzyme 2Antibodies, NeutralizingCell Culture TechniquesHumansPandemicsProtein BindingSARS-CoV-2Spike Glycoprotein, CoronavirusAngiotensin-Converting Enzyme 2Antibodies, NeutralizingSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2Cell culture medium-based biosensorCOVID-19Protein-protein interactionSARS-CoV-2Spike receptor-binding domain

Identifiers

PMID36827795
PMCPMC9938795
OpenAlexW4321349978

What OpenQuestion holds

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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.