| Literature DB >> 33501433 |
Yasunori Watanabe1,2, Luiza Mendonça3, Elizabeth R Allen4, Andrew Howe5, Mercede Lee4, Joel D Allen1, Himanshi Chawla1, David Pulido4, Francesca Donnellan4, Hannah Davies4, Marta Ulaszewska4, Sandra Belij-Rammerstorfer4,6, Susan Morris4, Anna-Sophia Krebs3, Wanwisa Dejnirattisai7, Juthathip Mongkolsapaya7,8,9, Piyada Supasa7, Gavin R Screaton7,10, Catherine M Green7, Teresa Lambe4,6, Peijun Zhang3,5, Sarah C Gilbert4,6, Max Crispin1.
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 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.Entities:
Year: 2021 PMID： 33501433 PMCID： PMC7836103 DOI： 10.1101/2021.01.15.426463
Source DB: PubMed Journal: bioRxiv