Evidence map›Paper›PMID 41770397›Full record

ArticleBiomedical microdevices2026

Nanoyeast-based impedimetric biosensor with mutated single chain antigen-binding fragment anchoring for SARS-CoV-2 detection.

Rafael Cintra Hensel, Elsa Maria Materón, Anna Julia Graboschi Macedo, Breno Vilas Boas Raimundo, Marco Antonio Seiki Kadowaki, Deivys Leandro Portuondo Fuentes, Alberto Gomes Tavares Junior, Letícia de Aquino Penteado, Cleslei Fernando Zanelli, Ricardo Bentes de Azevedo and 6 more

Abstract read
In one paragraph

Article in Biomedical microdevices, 2026. 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
–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

0 citing papers in PubMed.

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

16 authors.

Rafael Cintra HenselSão Carlos Institute of Physics, University of São Paulo - USP, São Carlos, 13560-970, São Paulo, Brazil.ORCID http://orcid.org/0000-0001-7060-6604
Elsa Maria MaterónSão Carlos Institute of Physics, University of São Paulo - USP, São Carlos, 13560-970, São Paulo, Brazil.ORCID http://orcid.org/0000-0002-3382-1193
Anna Julia Graboschi MacedoSchool of Pharmaceutical Sciences, São Paulo State University - UNESP, Araraquara, 14800-903, São Paulo, Brazil.ORCID http://orcid.org/0000-0002-2078-7782
Breno Vilas Boas RaimundoSchool of Pharmaceutical Sciences, São Paulo State University - UNESP, Araraquara, 14800-903, São Paulo, Brazil.ORCID http://orcid.org/0000-0003-3697-9380
Marco Antonio Seiki KadowakiSchool of Pharmaceutical Sciences, São Paulo State University - UNESP, Araraquara, 14800-903, São Paulo, Brazil.ORCID http://orcid.org/0000-0003-0188-2079
Deivys Leandro Portuondo FuentesSchool of Pharmaceutical Sciences, São Paulo State University - UNESP, Araraquara, 14800-903, São Paulo, Brazil.ORCID http://orcid.org/0000-0003-2678-0431
Alberto Gomes Tavares JuniorSchool of Pharmaceutical Sciences, São Paulo State University - UNESP, Araraquara, 14800-903, São Paulo, Brazil.ORCID http://orcid.org/0000-0002-6083-8177
Letícia de Aquino PenteadoSchool of Pharmaceutical Sciences, São Paulo State University - UNESP, Araraquara, 14800-903, São Paulo, Brazil.ORCID http://orcid.org/0000-0001-9592-7279
Cleslei Fernando ZanelliSchool of Pharmaceutical Sciences, São Paulo State University - UNESP, Araraquara, 14800-903, São Paulo, Brazil.ORCID http://orcid.org/0000-0001-7831-1149
Ricardo Bentes de AzevedoInstitute of Biological Sciences, University of Brasília - UNB, Brasília, 70910-900, Distrito Federal, Brazil.ORCID http://orcid.org/0000-0002-2137-9588
Marlus ChorilliSchool of Pharmaceutical Sciences, São Paulo State University - UNESP, Araraquara, 14800-903, São Paulo, Brazil.ORCID http://orcid.org/0000-0002-6698-0545
Alexandra Ivo de MedeirosSchool of Pharmaceutical Sciences, São Paulo State University - UNESP, Araraquara, 14800-903, São Paulo, Brazil.ORCID http://orcid.org/0000-0001-6048-3647
Emanuel CarrilhoSão Carlos Institute of Chemistry, University of São Paulo - USP, São Carlos, 13566-590, São Paulo, Brazil.ORCID http://orcid.org/0000-0001-7351-8220
Osvaldo N OliveiraSão Carlos Institute of Physics, University of São Paulo - USP, São Carlos, 13560-970, São Paulo, Brazil.ORCID http://orcid.org/0000-0002-5399-5860
Sandro Roberto ValentiniSchool of Pharmaceutical Sciences, São Paulo State University - UNESP, Araraquara, 14800-903, São Paulo, Brazil.ORCID http://orcid.org/0000-0003-4453-5413
Tatiana Maria Souza-MoreiraSchool of Pharmaceutical Sciences, São Paulo State University - UNESP, Araraquara, 14800-903, São Paulo, Brazil. tatiana.souza@unesp.br.ORCID http://orcid.org/0000-0001-8198-5232

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Impedimetric biosensors are useful for pathogen detection as they combine electrical impedance spectroscopy with the specificity of immunological reactions. These devices can be engineered to detect minute changes in electrical impedance caused by interactions between immobilized recognition elements and target antigens in a sample. They are advantageous in allowing for label-free and real-time detection, with the ability to operate without electroactive materials. Herein, we report an impedimetric biosensor containing nanoyeast expressing SARS-CoV-2 antibody fragments as the active layer. Using nanoyeast offers key advantages such as biocompatibility and stability. The single-chain antigen-binding fragment (scFab) against receptor binding domain of SARS-CoV-2 was mutated according to in silico predictions. It was expressed in Saccharomyces cerevisiae fused to the agglutinin 2 (Aga2), where the binding to Aga1 on the yeast cell wall displays the scFab on the surface of nanofragmented yeast (NY). Electrical impedance monitoring confirmed the successful immobilization of NY onto an adsorbed chitosan layer. This biosensor architecture detected SARS-CoV-2 spike protein with a limit of detection (LoD) of 5 × 10⁻¹⁸ g/mL. It distinguished viral concentrations ranging from 0.3 to 80 plaque-forming units per milliliter (PFU/mL) and demonstrated selectivity for SARS-CoV-2 over H1N1 influenza and Dengue virus. These findings suggest that this biosensing technology could be further adapted for other biomedical and clinical analyses, being promising to improve current pathogen detection methods.

Indexed as

Biosensing TechniquesCOVID-19MutationSARS-CoV-2Single-Chain AntibodiesDielectric SpectroscopyElectric ImpedanceHumansLimit of DetectionSaccharomyces cerevisiaeSpike Glycoprotein, CoronavirusSingle-Chain AntibodiesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Antibody antigen-binding fragmentCOVID-19Electrical impedance spectroscopySpike proteinYeast surface display

Identifiers

PMID41770397
PMCPMC12953393

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LicenceCC BY
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Registered trials

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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.