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Nanoluciferase complementation-based bioreporter reveals the importance of N-linked glycosylation of SARS-CoV-2 S for viral entry

Authors
  • Azad, Taha1, 2
  • Singaravelu, Ragunath1, 2
  • Taha, Zaid1, 2
  • Jamieson, Taylor R.1, 2
  • Boulton, Stephen1, 2
  • Crupi, Mathieu J.F.1, 2
  • Martin, Nikolas T.1, 2
  • Brown, Emily E.F.1, 2
  • Poutou, Joanna1, 2
  • Ghahremani, Mina3
  • Pelin, Adrian1, 2
  • Nouri, Kazem4
  • Rezaei, Reza1, 2
  • Marshall, Christopher Boyd4
  • Enomoto, Masahiro4
  • Arulanandam, Rozanne1
  • Alluqmani, Nouf1, 2
  • Samson, Reuben5, 6
  • Gingras, Anne-Claude5, 6
  • Cameron, D. William1, 2
  • And 4 more
  • 1 Center for Innovative Cancer Therapeutics, Ottawa Hospital Research Institute, Ottawa, ON K1H 8L6, Canada
  • 2 Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, ON K1H 8M5, Canada
  • 3 Department of Biology, University of Ottawa, Ottawa, ON K1N 6N5, Canada
  • 4 Princess Margaret Cancer Centre, University Health Network, Toronto, ON M5G 1L7, Canada
  • 5 Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, ON M5G 1X5, Canada
  • 6 Department of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada
  • 7 Department of Pathology and Molecular Medicine, Queens University, Kingston, ON K7L 3N6, Canada
Type
Published Article
Journal
Molecular Therapy
Publisher
Elsevier
Publication Date
Feb 10, 2021
Volume
29
Issue
6
Pages
1984–2000
Identifiers
DOI: 10.1016/j.ymthe.2021.02.007
PMID: 33578036
PMCID: PMC7872859
Source
PubMed Central
Keywords
Disciplines
  • Original Article
License
Unknown

Abstract

In this study, Azad et al. developed a nanoluciferase complementation reporter to interrogate the interaction between the SARS-CoV-2 viral spike protein and its host entry receptor. Using this bioreporter, they uncovered critical host and viral determinants of the interaction, including a role for glycosylation of asparagine residues within the RBD in mediating successful viral entry.

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