Evidence map›Paper›PMID 35380004›Full record

ArticleThe Biochemical journal2022

Development of a colorimetric assay for the detection of SARS-CoV-2 3CLpro activity.

Gavin D Garland, Robert F Harvey, Thomas E Mulroney, Mie Monti, Stewart Fuller, Richard Haigh, Pehuén Pereyra Gerber, Michael R Barer, Nicholas J Matheson, Anne E Willis

Abstract read
In one paragraph

Article in The Biochemical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

10 authors.

Gavin D GarlandMRC Toxicology Unit, Gleeson Building, Tennis Court Rd, Cambridge, U.K.
Robert F HarveyMRC Toxicology Unit, Gleeson Building, Tennis Court Rd, Cambridge, U.K.
Thomas E MulroneyMRC Toxicology Unit, Gleeson Building, Tennis Court Rd, Cambridge, U.K.
Mie MontiMRC Toxicology Unit, Gleeson Building, Tennis Court Rd, Cambridge, U.K.
Stewart FullerDepartment of Medicine, University of Cambridge, Cambridge, U.K.
Richard HaighDepartment of Respiratory Sciences, Maurice Shock Medical Sciences Building, University Road, Leicester, U.K.
Pehuén Pereyra GerberDepartment of Medicine, University of Cambridge, Cambridge, U.K.
Michael R BarerDepartment of Respiratory Sciences, Maurice Shock Medical Sciences Building, University Road, Leicester, U.K.
Nicholas J MathesonDepartment of Medicine, University of Cambridge, Cambridge, U.K.
Anne E WillisMRC Toxicology Unit, Gleeson Building, Tennis Court Rd, Cambridge, U.K.ORCID 0000-0002-1470-8531

Funding

Department of HealthMedical Research Council MC_UU_00025/7Medical Research Council MR/P008801/ 1Medical Research Council MR/P008801/1
6 · The paper itself

Abstract

Diagnostic testing continues to be an integral component of the strategy to contain the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) global pandemic, the causative agent of Coronavirus Disease 2019 (COVID-19). The SARS-CoV-2 genome encodes the 3C-like protease (3CLpro) which is essential for coronavirus replication. This study adapts an in vitro colorimetric gold nanoparticle (AuNP) based protease assay to specifically detect the activity of SARS-CoV-2 3CLpro as a purified recombinant protein and as a cellular protein exogenously expressed in HEK293T human cells. We also demonstrate that the specific sensitivity of the assay for SARS-CoV-2 3CLpro can be improved by use of an optimised peptide substrate and through hybrid dimerisation with inactive 3CLpro mutant monomers. These findings highlight the potential for further development of the AuNP protease assay to detect SARS-CoV-2 3CLpro activity as a novel, accessible and cost-effective diagnostic test for SARS-CoV-2 infection at the point-of-care. Importantly, this versatile assay could also be easily adapted to detect specific protease activity associated with other viruses or diseases conditions.

Indexed as

COVID-19Metal NanoparticlesAntiviral AgentsColorimetryCoronavirus 3C ProteasesGoldHEK293 CellsHumansPeptide HydrolasesProtease InhibitorsSARS-CoV-2Antiviral AgentsCoronavirus 3C ProteasesGoldPeptide HydrolasesProtease Inhibitorsassay developmentCoronavirusCOVID 19

Identifiers

PMID35380004
PMCPMC9162461

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.