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• W3099050566 abstract "ABSTRACT 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." @default.
• W3099050566 created "2020-11-23" @default.
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• W3099050566 date "2020-11-18" @default.
• W3099050566 modified "2023-10-12" @default.
• W3099050566 title "An engineered receptor-binding domain improves the immunogenicity of multivalent SARS-CoV-2 vaccines" @default.
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• W3099050566 doi "https://doi.org/10.1101/2020.11.18.388934" @default.
• W3099050566 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7685318" @default.
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• W3099050566 hasPublicationYear "2020" @default.
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