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

. CC-BY-NC-ND 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.05.026377 doi: bioRxiv preprint Another important aspect is the evaluation of putative mAbs that could bind to the RBD of the new SARS-CoV-2. Following the work of Tian and collaborators, 8 we investigated the interactions between the two SARS S RBD proteins with some of the most potent SARS-CoV-1 S RBD specific neutralizing antibodies (80R, F26G19, m396, CR3022). Figure 6 shows the free energy profiles at the acid regime and physiological salt conditions. For all studied fragments of Abs, a relatively stronger attraction is always observed for the S RBD protein from the SARS-CoV-1 interacting with any of these mAbs. This can be better seen in Figure 6b Moreover, the work of Tian and co-authors suggested that only for CR3022 it was experimentally measured a reasonable binding. 8 The combination of these information could indicate that a threshold of −0.67KBT for βwmin can be used to better refine the theoretical binding predictions of these macromolecular complexations (i.e. all viral protein-protein systems with a value of βwmin smaller than −0.67KBT are expected to experience binding in vivo at least). Table S1 summarizes the values of βwmin given between parenthesis. The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.05.026377 doi: bioRxiv preprint The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.05.026377 doi: bioRxiv preprint