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?:abstract
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The SARS-coronavirus 2 (SARS-CoV-2) spike (S) protein mediates viral entry into cells expressing the angiotensin-converting enzyme 2 (ACE2). The S protein engages ACE2 through its receptor-binding domain (RBD), an independently folded 197-amino acid fragment of the 1273-amino acid S-protein protomer. The RBD is the primary SARS-CoV-2 neutralizing epitope and a critical target of any SARS-CoV-2 vaccine. Here we show that this RBD conjugated to each of two carrier proteins elicited more potent neutralizing responses in immunized rodents than did a similarly conjugated proline-stabilized S-protein ectodomain. Nonetheless, the native RBD expresses inefficiently, limiting its usefulness as a vaccine antigen. However, we show that an RBD engineered with four novel glycosylation sites (gRBD) expresses markedly more efficiently, and generates a more potent neutralizing responses as a DNA vaccine antigen, than the wild-type RBD or the full-length S protein, especially when fused to multivalent carriers such as an H. pylori ferritin 24-mer. Further, gRBD is more immunogenic than the wild-type RBD when administered as a subunit protein vaccine. Our data suggest that multivalent gRBD antigens can reduce costs and doses, and improve the immunogenicity, of all major classes of SARS-CoV-2 vaccines.
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?:creator
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?:doi
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10.1101/2020.11.18.388934
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?:doi
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?:journal
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?:license
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?:pdf_json_files
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document_parses/pdf_json/de70419b587260918e928f8f2c2bc23bfba4694b.json; document_parses/pdf_json/731426f3fb691d5f7f62f9f29706827a7f896cd1.json
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document_parses/pmc_json/PMC7685318.xml.json
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?:pmid
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?:pmid
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?:source
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BioRxiv; Medline; PMC; WHO
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?:title
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An engineered receptor-binding domain improves the immunogenicity of multivalent SARS-CoV-2 vaccines
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