On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2 spike proteins with monoclonal antibodies and the receptor ACE2

Carolina Corrêa Giron; Aatto Laaksonen; Fernando L. Barroso da Silva

Finally, we compared the EE predictions for CR3022' (34 aa) with CR3022 (33 aa) interacting with SARS-CoV-2 S RBD protein − see Figure 10 . The predicted EEs for the interaction with CR3022' are essentially the same ones observed for CR3022 (27 common aa) . This implies that the suggested mutations here do not affected the antigenic regions. Another particularly interesting feature of this computer-designed molecule is that the number of EEs shared with ACE2 has increased from 18 (for CR3022) to 27 (for CR3022'). This might amplify the potential of this mAb candidate to better block the virus-host cell interaction. CR3022' by the electrostatic method. Data for CR3022 is the same shown in Figure 9 . All other details are also as in Figure 9 .