Author: Ivan Mercurio; Vincenzo Tragni; Francesco Busco; Anna De Grassi; Ciro Leonardo Pierri
Title: Protein structure analysis of the interactions between SARS-CoV-2 spike protein and the human ACE2 receptor: from conformational changes to novel neutralizing antibodies Document date: 2020_4_18
ID: mswmkgl4_45
Snippet: Due to the uncertain data concerning fusion events and mechanism of action of S230 antibody, we built a new SARS-CoV-1/2 RBD directed antibody starting from the analysis of monomer-monomer interface interactions observed between the m396 antibody crystallized in complex with SARS-CoV-1 RBD (44), superimposed to SARS-CoV-1 spike RBD / ACE2 complex (2ajf.pdb), and by comparing them with monomer-monomer interface interactions observed between the mo.....
Document: Due to the uncertain data concerning fusion events and mechanism of action of S230 antibody, we built a new SARS-CoV-1/2 RBD directed antibody starting from the analysis of monomer-monomer interface interactions observed between the m396 antibody crystallized in complex with SARS-CoV-1 RBD (44), superimposed to SARS-CoV-1 spike RBD / ACE2 complex (2ajf.pdb), and by comparing them with monomer-monomer interface interactions observed between the modelled m396 antibody in complex with SARS-CoV-2 RBD, superimposed to SARS-CoV-2 RBD/ACE2 (6vw1.pdb; 6lzg.pdb) protein complex (Fig. 7) . Then, we highlighted m396 CDR residues (Tab. 2) for replacing them aiming to increase m392 affinity versus SARS-CoV-1/2 spike RBDs. Residues to be mutated/replaced were chosen according author/funder. All rights reserved. No reuse allowed without permission.
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