All RBD and ACE2 molecules are shown in individual colored cartoons. This substitution has been found in SARS-CoV-2 human samples and others of unknown origin ]. In this work, we study the molecular bases that underlie the enhanced adherence to ACE2 conferred by the mutation Q498Y, located in the SARS-CoV-2 spike receptor binding domain (RBD). Further, some mutations can ultimately lead to immune evasion and reduction of the efficacy of existing vaccines. Most of them harbor amino acid mutations in the spike protein with the potential to modulate the strength of the spike:ACE2 interaction. Since its initial identification, a remarkable number of variants and other yet unmonitored lineages have been detected. SARS-CoV-2 initiates infection of host cells by anchoring its viral envelope spike protein to the ACE2 receptor on the surface of human cells.
Structural bases for the higher adherence to ACE2 conferred by the SARS-CoV-2 spike Q498Y substitutionĮlena Erausquin, Fabian Glaser, Juan Fernández-Recio, Jacinto López-Sagaseta
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