coronavirus neutralizing antibody

Modeled SP1-77 binding site on various SARS-CoV-2 variants. (A) The potential footprint of SP1-77 on the modeled RBDs from different SARS-CoV-2 variants in a top view. The RBD was shown in surface representation in gray with the SP1-77 footprint highlighted in green and the mutations in each variant in blue. The Fv region of SP1-77 was shown in ribbon diagram in green. Most mutations on spike variants were not located at the SP1-77 footprint. (B) Side view of a selected panel from A. (C) Structural comparison of the SP1-77 binding interface among the RBDs of wildtype G614, Mu and Omicron variants. The conservative mutation Arg346Lys in Mu preserved the salt bridge between the residue 346 in the RBD and the SP1-77 Asp95. The mutations in Omicron variant reconfigured the local conformation near the N343-glycan, which is on the edge of SP1-77 footprint. The RBD was colored in gray, the SP1-77 heavy chain was colored in green and the light chain was colored in light green. Mutations in the Mu and Omicron variants were shown in stick and ball model in blue.
A new broadly neutralizing antibody neutralizes all known coronavirus variants