Structure-activity relationships of B.1.617 and other SARS-CoV-2 spike variants
Yang, T.-J.; Yu, P.-Y.; Chang, Y.-C.; Chang, N.-E.; Tsai, Y.-X.; Liang, K.-H.; Draczkowski, P.; Lin, B.; Wang, Y.-S.; Chien, Y.-C.; Khoo, K.-H.; Wu, H.-C.; Hsu, S.-T. D.
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The surge of COVID-19 infection cases is spurred by emerging SARS-CoV-2 variants such as B.1.617. Here we report 38 cryo-EM structures, corresponding to the spike protein of the Beta (B.1.351), Gamma (P.1), Delta (B.1.617.2) and Kappa (B.1.617.1) variants in different functional states with and without its receptor, ACE2. Mutations on the N-terminal domain not only alter the conformation of the highly antigenic supersite of the Delta variant, but also remodel the glycan shield by deleting or adding N-glycans of the Delta and Gamma variants, respectively. Substantially enhanced ACE2 binding was observed for all variants, whose mutations on the receptor binding domain modulate the electrostatics of the binding interfaces. Despite their abilities to escape host immunity, all variants can be potently neutralized by three unique antibodies.
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