ArticleJournal of immunological methods2022
Non-glycosylated SARS-CoV-2 RBD elicited a robust neutralizing antibody response in mice.
Article in Journal of immunological methods, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Development of an in vitro method to assess the immunogenicity of biologics in the prevention of infectious diseases.Immunologic research · 2025Article
- Review
- A protein vaccine of RBD integrated with immune evasion mutation shows broad protection against SARS-CoV-2.Signal transduction and targeted therapy · 2024Article
- Novel Affibody Molecules Specifically Bind to SARS-CoV-2 Spike Protein and Efficiently Neutralize Delta and Omicron Variants.Microbiology spectrum · 2023Article
- Article
- Article
- Functional Expression of the Recombinant Spike Receptor Binding Domain of SARS-CoV-2 Omicron in the Periplasm ofBioengineering (Basel, Switzerland) · 2022Article
- Recombinant expression of SARS-CoV-2 receptor binding domain (RBD) inIranian journal of basic medical sciences · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycosylated receptor-binding domain (glycoRBD) of SARS-CoV-2 can induce protective neutralizing antibodies to function as a vaccine. However, it is unclear whether vaccines using non-glycosylated RBD (non-glycoRBD) can induce protective immunity. Here, we report the efficacy of a SARS-CoV-2 non-glycoRBD vaccine produced by prokaryotic system in mice. The recombinant non-glycoRBD protein was overexpressed in Escherichia coli in the form of inclusion bodies, and was obtained after renaturation and three-step purification. From HPLC analysis, the purity of the RBD was 99%. Additionally, angiotensin converting enzyme 2 (ACE2)-binding assays revealed that E.coli-derived non-glycoRBD had binding activity consistent with glycoRBD. The RBD was formulated with CpG ODN and Al(OH)
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Registered trials
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