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Title | Native-like SARS-CoV-2 spike glycoprotein expressed by ChAdOx1 nCoV-19/AZD1222 vaccine. |
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Journal, issue, pages | bioRxiv, Year 2021 |
Publish date | Jan 19, 2021 |
Authors | Yasunori Watanabe / Luiza Mendonça / Elizabeth R Allen / Andrew Howe / Mercede Lee / Joel D Allen / Himanshi Chawla / David Pulido / Francesca Donnellan / Hannah Davies / Marta Ulaszewska / Sandra Belij-Rammerstorfer / Susan Morris / Anna-Sophia Krebs / Wanwisa Dejnirattisai / Juthathip Mongkolsapaya / Piyada Supasa / Gavin R Screaton / Catherine M Green / Teresa Lambe / Peijun Zhang / Sarah C Gilbert / Max Crispin / |
PubMed Abstract | Vaccine development against the SARS-CoV-2 virus focuses on the principal target of the neutralizing immune response, the spike (S) glycoprotein. Adenovirus-vectored vaccines offer an effective ...Vaccine development against the SARS-CoV-2 virus focuses on the principal target of the neutralizing immune response, the spike (S) glycoprotein. Adenovirus-vectored vaccines offer an effective platform for the delivery of viral antigen, but it is important for the generation of neutralizing antibodies that they produce appropriately processed and assembled viral antigen that mimics that observed on the SARS-CoV-2 virus. Here, we describe the structure, conformation and glycosylation of the S protein derived from the adenovirus-vectored ChAdOx1 nCoV-19/AZD1222 vaccine. We demonstrate native-like post-translational processing and assembly, and reveal the expression of S proteins on the surface of cells adopting the trimeric prefusion conformation. The data presented here confirms the use of ChAdOx1 adenovirus vectors as a leading platform technology for SARS-CoV-2 vaccines. |
External links | bioRxiv / PubMed:33501433 / PubMed Central |
Methods | EM (subtomogram averaging) |
Resolution | 11.6 Å |
Structure data | EMDB-12530: |