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Native-like SARS-CoV-2 Spike Glycoprotein Expressed by ChAdOx1 nCoV-19/AZD1222 Vaccine.
Watanabe, Yasunori; Mendonça, Luiza; Allen, Elizabeth R; Howe, Andrew; Lee, Mercede; Allen, Joel D; Chawla, Himanshi; Pulido, David; Donnellan, Francesca; Davies, Hannah; Ulaszewska, Marta; Belij-Rammerstorfer, Sandra; Morris, Susan; Krebs, Anna-Sophia; Dejnirattisai, Wanwisa; Mongkolsapaya, Juthathip; Supasa, Piyada; Screaton, Gavin R; Green, Catherine M; Lambe, Teresa; Zhang, Peijun; Gilbert, Sarah C; Crispin, Max.
  • Watanabe Y; School of Biological Sciences, University of Southampton, Southampton, SO17 1BJ, U.K.
  • Mendonça L; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, U.K.
  • Allen ER; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, Oxford, OX3 7BN, U.K.
  • Howe A; The Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, U.K.
  • Lee M; Electron Bio-imaging Centre, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, U.K.
  • Allen JD; The Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, U.K.
  • Chawla H; School of Biological Sciences, University of Southampton, Southampton, SO17 1BJ, U.K.
  • Pulido D; School of Biological Sciences, University of Southampton, Southampton, SO17 1BJ, U.K.
  • Donnellan F; The Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, U.K.
  • Davies H; The Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, U.K.
  • Ulaszewska M; The Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, U.K.
  • Belij-Rammerstorfer S; The Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, U.K.
  • Morris S; The Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, U.K.
  • Krebs AS; NIHR Oxford Biomedical Research Centre, Oxford, U.K.
  • Dejnirattisai W; The Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, U.K.
  • Mongkolsapaya J; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, Oxford, OX3 7BN, U.K.
  • Supasa P; The Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, U.K.
  • Screaton GR; The Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, U.K.
  • Green CM; Dengue Hemorrhagic Fever Research Unit, Office for Research and Development, Faculty of Medicine, Siriraj Hospital, Mahidol University, Bangkok, Thailand.
  • Lambe T; Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, U.K.
  • Zhang P; The Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, U.K.
  • Gilbert SC; The Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, U.K.
  • Crispin M; Division of Medical Sciences, John Radcliffe Hospital, University of Oxford, Oxford, U.K.
ACS Cent Sci ; 7(4): 594-602, 2021 Apr 28.
Article in English | MEDLINE | ID: covidwho-1225486
Preprint
This scientific journal article is probably based on a previously available preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
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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 confirm the use of ChAdOx1 adenovirus vectors as a leading platform technology for SARS-CoV-2 vaccines.
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Full text: Available Collection: International databases Database: MEDLINE Topics: Vaccines Language: English Journal: ACS Cent Sci Year: 2021 Document Type: Article Affiliation country: Acscentsci.1c00080

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Full text: Available Collection: International databases Database: MEDLINE Topics: Vaccines Language: English Journal: ACS Cent Sci Year: 2021 Document Type: Article Affiliation country: Acscentsci.1c00080