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Two Receptor Binding Strategy of SARS-CoV-2 is mediated by both the n-terminal and Receptor-binding Spike Domain
The Journal of Physical Chemistry B 2024
Monti, Michele & Milanetti, Edoardo & Frans, Myrthe & Miotto, Mattia & Rienzo, Lorenzo & Baranov, Maksim & Gosti, Giorgio & Somavarapu, Arun & Nagaraj, Madhu & Golbek, Thaddeus & Rossing, Emiel & Moons, Sam & Boltje, Thomas & Bogaart, Geert & Weidner, Tobias & Otzen, Daniel & Tartaglia, Gian & Ruocco, Giancarlo & Roeters, Steven.
This study investigated why SARS-CoV-2 spreads faster than related β-coronaviruses, testing whether its spike protein uses a two-receptor strategy involving both sialic acid (SA) and ACE2. Combining molecular-dynamics simulations, binding-site analysis and experiments, the authors showed both the N-terminal domain and the receptor-binding domain of the spike bind SA, and that SA anchoring enhances ACE2 binding. Flow Induced Dispersion Analysis (FIDA) was used to validate the interaction by measuring the binding of fluorescently labeled spike S1 to SA-containing glycolipid vesicles and estimating dissociation constants. It is an example of using FIDA to measure protein–glycolipid binding affinity in solution.
