ArticlePloS one2019
Protein refolding based on high hydrostatic pressure and alkaline pH: Application on a recombinant dengue virus NS1 protein.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Human growth hormone inclusion bodies present native-like secondary and tertiary structures which can be preserved by mild solubilization for refolding.Microbial cell factories · 2022Article
- Recombinant PilS: Cloning, Expression and Biochemical Characterization of a Pil-Fimbriae Subunit.Microorganisms · 2022Article
- Development of a plant-produced recombinant monoclonal antibody against Δ-9-tetrahydrocannabinol (Δ9-THC) for immunoassay application.Biotechnology reports (Amsterdam, Netherlands) · 2022Article
- Article
- Solubilization and Refolding of Inclusion Body Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Anti-Flavivirus Vaccines: Review of the Present Situation and Perspectives of Subunit Vaccines Produced inVaccines · 2020Review
- Article
- Optimization and scale-up production of Zika virus ΔNS1 in Escherichia coli: application of Response Surface Methodology.AMB Express · 2019Article
- Transient Expression of Dengue Virus NS1 Antigen inFrontiers in plant science · 2019Article
- Natural versus Recombinant Viral Antigens in SARS-CoV-2 Serology: Challenges in Optimizing Laboratory Diagnosis of COVID-19.Clinics (Sao Paulo, Brazil)Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study we evaluated the association of high hydrostatic pressure (HHP) and alkaline pH as a minimally denaturing condition for the solubilization of inclusion bodies (IBs) generated by recombinant proteins expressed by Escherichia coli strains. The method was successfully applied to a recombinant form of the dengue virus (DENV) non-structural protein 1 (NS1). The minimal pH for IBs solubilization at 1 bar was 12 while a pH of 10 was sufficient for solubilization at HHP: 2.4 kbar for 90 min and 0.4 kbar for 14 h 30 min. An optimal refolding condition was achieved by compression of IBs at HHP and pH 10.5 in the presence of arginine, oxidized and reduced glutathiones, providing much higher yields (up to 8-fold) than association of HHP and GdnHCl via an established protocol. The refolded NS1, 109 ± 9.5 mg/L bacterial culture was recovered mainly as monomer and dimer, corresponding up to 90% of the total protein and remaining immunologically active. The proposed conditions represent an alternative for the refolding of immunologically active recombinant proteins expressed as IBs.
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Registered trials
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.