Fig. 6: Effects of mutations on viral fusion by in silico modeling. | Communications Biology

Fig. 6: Effects of mutations on viral fusion by in silico modeling.

From: SARS-CoV-2 omicron variants harbor spike protein mutations responsible for their attenuated fusogenic phenotype

Fig. 6: Effects of mutations on viral fusion by in silico modeling.The alternative text for this image may have been generated using AI.

a Ribbon representation of the BA.1 spike monomer protein in the close conformation. S1 domain is shown in blue and S2 domain is shown in grey. The mutations are rendered in balls and colored in red, blue and brown for the O, N, and C atoms, respectively. b Mutation of T547K in the WT and BA.1. The trimer proteins are shown in ribbons in grey (S2) and cyan (S1). The H-bond formed between K547 and D389 in BA.1 is shown in red dotted line. c Mutation of H655Y at the S1/S2 cleavage site (G614). The aromatic stacking interaction between H655Y and F643 is shown, whereas an additional H-bond is formed between Y655 and T696 in the BA.1. d Mutation of N856K observed in the Wuhan and BA.1 variant. K856 forms a salt bridge with D568. e Mutation of Q954H in the Wuhan and BA.1. Q954 but not H954 forms an H-bond with R1014. f Mutations of Q954H, N969K, and L981F in the HR1 domain (grey) and form H-bond interactions with residues of the HR2 domain (cyan) in the postfusion 6HB structure.

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