posted on 2021-04-02, 20:29authored byYasunori 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
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 confirm the use of ChAdOx1 adenovirus vectors as a leading platform
technology for SARS-CoV-2 vaccines.