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Site-Specific Steric Control of SARS-CoV-2 Spike Glycosylation.
Allen, Joel D; Chawla, Himanshi; Samsudin, Firdaus; Zuzic, Lorena; Shivgan, Aishwary Tukaram; Watanabe, Yasunori; He, Wan-Ting; Callaghan, Sean; Song, Ge; Yong, Peter; Brouwer, Philip J M; Song, Yutong; Cai, Yongfei; Duyvesteyn, Helen M E; Malinauskas, Tomas; Kint, Joeri; Pino, Paco; Wurm, Maria J; Frank, Martin; Chen, Bing; Stuart, David I; Sanders, Rogier W; Andrabi, Raiees; Burton, Dennis R; Li, Sai; Bond, Peter J; Crispin, Max.
  • Allen JD; School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, U.K.
  • Chawla H; School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, U.K.
  • Samsudin F; Bioinformatics Institute, Agency for Science, Technology and Research (A*STAR), Singapore 138671.
  • Zuzic L; Bioinformatics Institute, Agency for Science, Technology and Research (A*STAR), Singapore 138671.
  • Shivgan AT; Department of Chemistry, Faculty of Science and Engineering, Manchester Institute of Biotechnology, The University of Manchester, Manchester M1 7DN, U.K.
  • Watanabe Y; Bioinformatics Institute, Agency for Science, Technology and Research (A*STAR), Singapore 138671.
  • He WT; Department of Biological Sciences, National University of Singapore, Singapore 117543.
  • Callaghan S; School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, U.K.
  • Song G; Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, California 92037, United States.
  • Yong P; IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, California 92037, United States.
  • Brouwer PJM; Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, California 92037, United States.
  • Song Y; Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, California 92037, United States.
  • Cai Y; IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, California 92037, United States.
  • Duyvesteyn HME; Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, California 92037, United States.
  • Malinauskas T; Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, California 92037, United States.
  • Kint J; IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, California 92037, United States.
  • Pino P; Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, California 92037, United States.
  • Wurm MJ; Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, California 92037, United States.
  • Frank M; IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, California 92037, United States.
  • Chen B; Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, California 92037, United States.
  • Stuart DI; Department of Medical Microbiology, Amsterdam UMC, University of Amsterdam, Amsterdam Infection & Immunity Institute, 1007 MB Amsterdam, The Netherlands.
  • Sanders RW; Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
  • Andrabi R; Beijing Advanced Innovation Center for Structural Biology and Frontier Research Center for Biological Structure, Beijing 100084, China.
  • Burton DR; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, Massachusetts 02115, United States.
  • Li S; Division of Structural Biology, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford OX3 7BN, U.K.
  • Bond PJ; Division of Structural Biology, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford OX3 7BN, U.K.
  • Crispin M; ExcellGene SA, CH1870 Monthey, Switzerland.
Biochemistry ; 60(27): 2153-2169, 2021 07 13.
Article in English | MEDLINE | ID: covidwho-1387101
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ABSTRACT
A central tenet in the design of vaccines is the display of native-like antigens in the elicitation of protective immunity. The abundance of N-linked glycans across the SARS-CoV-2 spike protein is a potential source of heterogeneity among the many different vaccine candidates under investigation. Here, we investigate the glycosylation of recombinant SARS-CoV-2 spike proteins from five different laboratories and compare them against S protein from infectious virus, cultured in Vero cells. We find patterns that are conserved across all samples, and this can be associated with site-specific stalling of glycan maturation that acts as a highly sensitive reporter of protein structure. Molecular dynamics simulations of a fully glycosylated spike support a model of steric restrictions that shape enzymatic processing of the glycans. These results suggest that recombinant spike-based SARS-CoV-2 immunogen glycosylation reproducibly recapitulates signatures of viral glycosylation.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Protein Conformation / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Topics: Vaccines Limits: Animals / Humans Language: English Journal: Biochemistry Year: 2021 Document Type: Article Affiliation country: ACS.BIOCHEM.1C00279

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Protein Conformation / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Topics: Vaccines Limits: Animals / Humans Language: English Journal: Biochemistry Year: 2021 Document Type: Article Affiliation country: ACS.BIOCHEM.1C00279