ArticleProtein expression and purification2021
Expression of SARS-CoV-2 surface glycoprotein fragment 319-640 in E. coli, and its refolding and purification.
Article in Protein expression and purification, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- Escherichia coli Nissle 1917 efficiently expresses the RBD domain of SARS-CoV-2 spike protein without codon optimization.Scientific reports · 2025Article
- Amyloidogenesis of SARS-CoV-2 delta plus and omicron variants receptor-binding domain (RBD): impact of SUMO fusion tag.Biotechnology letters · 2024Article
- Review
- Expression and purification of the receptor-binding domain of SARS-CoV-2 spike protein in mammalian cells for immunological assays.FEBS open bio · 2024Article
- Oral administration of a recombinant modified RBD antigen of SARS-CoV-2 as a possible immunostimulant for the care of COVID-19.Microbial cell factories · 2024Article
- Article
- RecombinantVeterinary world · 2023Article
- Utilization of Receptor-Binding Domain of SARS-CoV-2 Spike Protein Expressed in Escherichia coli for the Development of Neutralizing Antibody Assay.Molecular biotechnology · 2023Article
- A Novel Fusion Protein System for the Production of Nanobodies and the SARS-CoV-2 Spike RBD in a Bacterial System.Bioengineering (Basel, Switzerland) · 2023Article
- Enhancing neutralizing antibodies against receptor binding domain of SARS-CoV-2 by a safe natural adjuvant system.Virus research · 2023Article
- The main protease 3CLpro of the SARS-CoV-2 virus: how to turn an enemy into a helper.Frontiers in bioengineering and biotechnology · 2023Article
- Article
- Functional Expression of the Recombinant Spike Receptor Binding Domain of SARS-CoV-2 Omicron in the Periplasm ofBioengineering (Basel, Switzerland) · 2022Article
- A magnetic bead immunoassay to detect high affinity human IgG reactive to SARS-CoV-2 Spike S1 RBD produced in Escherichia coli.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2022Article
- Production and characterization of chimeric SARS-CoV-2 antigens based on the capsid protein of cowpea chlorotic mottle virus.International journal of biological macromolecules · 2022Article
- Addition of arginine hydrochloride and proline to the culture medium enhances recombinant protein expression in Brevibacillus choshinensis: The case of RBD of SARS-CoV-2 spike protein and its antibody.Protein expression and purification · 2022Article
- Expression, purification and characterization of SARS-CoV-2 spike RBD in ExpiCHO cells.Protein expression and purification · 2022Article
- Designed SARS-CoV-2 receptor binding domain variants form stable monomers.Biotechnology journal · 2022Article
- Escherichia coli recombinant expression of SARS-CoV-2 protein fragments.Microbial cell factories · 2022Article
- Production of the SARS-CoV-2 Spike protein and its Receptor Binding Domain in plant cell suspension cultures.Frontiers in plant science · 2022Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sensitive and specific serology tests are essential for epidemiological and public health studies of COVID-19 and for vaccine efficacy testing. The presence of antibodies to SARS-CoV-2 surface glycoprotein (Spike) and, specifically, its receptor-binding domain (RBD) correlates with inhibition of SARS-CoV-2 binding to the cellular receptor and viral entry into the cells. Serology tests that detect antibodies targeting RBD have high potential to predict COVID-19 immunity and to accurately determine the extent of the vaccine-induced immune response. Cost-effective methods of expression and purification of Spike and its fragments that preserve antigenic properties are essential for development of such tests. Here we describe a method of production of His6-tagged S319-640 fragment containing RBD in E. coli. It includes expression of the fragment, solubilization of inclusion bodies, and on-the-column refolding. The antigenic properties of the resulting product are similar, but not identical to the RBD-containing fragment expressed in human cells.
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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.