{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ke Q"],"funding":["National Key Research and Development Program of China"],"pagination":["113279"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9075978"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["506"],"pubmed_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)<sub>3</sub> ad"],"journal":["Journal of immunological methods"],"pubmed_title":["Non-glycosylated SARS-CoV-2 RBD elicited a robust neutralizing antibody response in mice."],"pmcid":["PMC9075978"],"funding_grant_id":["2020YFC0841400–008"],"pubmed_authors":["Wu J","Sun P","Mi T","Wang T","Ke Q","Liu B","Xu H"],"additional_accession":[]},"is_claimable":false,"name":"Non-glycosylated SARS-CoV-2 RBD elicited a robust neutralizing antibody response in mice.","description":"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)<sub>3</sub> ad","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jul","modification":"2025-04-04T10:02:23.596Z","creation":"2025-04-04T10:02:23.596Z"},"accession":"S-EPMC9075978","cross_references":{"pubmed":["35533747"],"doi":["10.1016/j.jim.2022.113279"]}}