| Download | - View final version: Impact of the temperature on the interactions between common variants of the SARS-CoV-2 receptor binding domain and the human ACE2 (PDF, 1.6 MiB)
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| DOI | Resolve DOI: https://doi.org/10.1038/s41598-022-15215-5 |
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| Author | Search for: Forest-Nault, Catherine1; Search for: Koyuturk, Izel1; Search for: Gaudreault, Jimmy; Search for: Pelletier, Alex1; Search for: L'Abbé, Denis1; Search for: Cass, Brian1; Search for: Bisson, Louis1; Search for: Burlacu, Alina1; Search for: Delafosse, Laurence1; Search for: Stuible, Matthew1; Search for: Henry, Olivier; Search for: De Crescenzo, Gregory; Search for: Durocher, Yves1 |
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| Affiliation | - National Research Council of Canada. Human Health Therapeutics
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| Funder | Search for: Natural Sciences and Engineering Research Council of Canada; Search for: National Research Council of Canada; Search for: Canada First Research Excellence Fund |
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| Format | Text, Article |
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| Physical description | 11 p. |
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| Abstract | Several key mutations in the Spike protein receptor binding domain (RBD) have been identified to influence its affinity for the human Angiotensin-Converting Enzyme 2 (ACE2). Here, we perform a comparative study of the ACE2 binding to the wild type (Wuhan) RBD and some of its variants: Alpha B.1.1.7, Beta B.1.351, Delta B.1.617.2, Kappa B.1.617.1, B.1.1.7 + L452R and Omicron B.1.1.529. Using a coiled-coil mediated tethering approach of ACE2 in a novel surface plasmon resonance (SPR)-based assay, we measured interactions at different temperatures. Binding experiments at 10 °C enhanced the kinetic dissimilarities between the RBD variants and allowed a proper fit to a Langmuir 1:1 model with high accuracy and reproducibility, thus unraveling subtle differences within RBD mutants and ACE2 glycovariants. Our study emphasizes the importance of SPR-based assay parameters in the acquisition of biologically relevant data and offers a powerful tool to deepen our understanding of the role of the various RBD mutations in ACE2 interaction binding parameters. |
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| Publication date | 2022-07-07 |
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| Publisher | Nature Research |
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| Licence | |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| Identifier | 15215 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 2b12c2d2-c415-4eda-88ff-98fe8308e5ad |
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| Record created | 2022-07-11 |
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| Record modified | 2023-03-16 |
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