Author: Carolina Corrêa Giron; Aatto Laaksonen; Fernando L. Barroso da Silva
Title: 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 Document date: 2020_4_10
ID: 4mv6qwpc_29
Snippet: "DYSVLYNSTFFSTFKCYG" for SARS-CoV-1 and "DYSVLYNSASFSTFKCYG" for SARS-CoV-2). A replacement of an amino acid from the same physical chemical group (e.g. D by E) can be enough to result in different interactions (e.g. "KGDDVRQIA" for SARS-CoV-1 and "RGDEVRQIA" for SARS-CoV-2). CR3022 perturbed more titratable groups: 27 for SARS-CoV-1 and 33 for SARS-CoV-2. Taking into account what was hypothesized for ACE2 above, this might be an addition contrib.....
Document: "DYSVLYNSTFFSTFKCYG" for SARS-CoV-1 and "DYSVLYNSASFSTFKCYG" for SARS-CoV-2). A replacement of an amino acid from the same physical chemical group (e.g. D by E) can be enough to result in different interactions (e.g. "KGDDVRQIA" for SARS-CoV-1 and "RGDEVRQIA" for SARS-CoV-2). CR3022 perturbed more titratable groups: 27 for SARS-CoV-1 and 33 for SARS-CoV-2. Taking into account what was hypothesized for ACE2 above, this might be an addition contribution to improve the capability of this mAb to interact and inhibit the RBD proteins. In fact, the experimental work of Tian and colleagues 8 do show that the CR3022 binding to SARS-CoV-2 S RBD is not affected by ACE2. This might be the molecular basis for this behavior. We are careful with the use of stronger statements here due to the limitation of the theoretical approach. Several additional issues remain to be further investigated.
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