Open AccessNative-like SARS-CoV-2 Spike Glycoprotein Expressed by ChAdOx1 nCoV-19/AZD1222 Vaccine
Author(s) -
Yasunori Watanabe,
L.G.D. Mendonça,
Elizabeth Allen,
Andrew Howe,
Mercede Lee,
Joel D. Allen,
Himanshi Chawla,
David Pulido,
Francesca R. Donnellan,
H. Dele Davies,
Marta Ulaszewska,
Sandra BelijRammerstorfer,
Susan Morris,
Anna-Sophia Krebs,
Wanwisa Dejnirattisai,
Juthathip Mongkolsapaya,
Piyada Supasa,
Gavin Screaton,
Catherine Green,
Teresa Lambe,
Peijun Zhang,
Sarah C. Gilbert,
Max Crispin
Publication year - 2021
Publication title -
acs central science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.893
H-Index - 76
eISSN - 2374-7951
pISSN - 2374-7943
DOI - 10.1021/acscentsci.1c00080
Subject(s) - glycoprotein , virology , glycosylation , covid-19 , antibody , virus , biology , neutralizing antibody , coronavirus , antigen , medicine , immunology , microbiology and biotechnology , infectious disease (medical specialty) , biochemistry , disease , pathology
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.