Extended Data Fig. 5: Lambda mutations mapping on known antibody recognition epitopes. | Nature Microbiology

Extended Data Fig. 5: Lambda mutations mapping on known antibody recognition epitopes.

From: Differential neutralizing antibody responses elicited by CoronaVac and BNT162b2 against SARS-CoV-2 Lambda in Chile

Extended Data Fig. 5

(a) X-ray structure (PDBid:7BWJ) of a complex between wild type RBD from SARS-CoV2 and the monoclonal antibody P2B-2F6, isolated from B-cells from an infected individual. b) Close up on the hydrophobic interactions established by L452 and F490 in the protein-protein interface. Mutations to polar amino acids as L452Q, F490S clearly disrupt the hydrophobic interface. c) Same as a) for antibody S2M28 solved by CryoEM (PDBid:7LY0), which recognizes the highly antigenic segment of the NTD domain. d) The close-up highlights the NTD-antibody interaction L249-I93. The deletion 246-252 would completely abrogate the binding by drastically reducing the binding epitope.

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