Author: Ilda D’Annessa; Filippo Marchetti; Giorgio Colombo
Title: Differential Antibody Recognition by Novel SARS-CoV-2 and SARS-CoV Spike Protein Receptor Binding Domains: Mechanistic Insights and Implications for the Design of Diagnostics and Therapeutics Document date: 2020_3_14
ID: c08ptb1o_14
Snippet: Importantly, after we ran our predictions on the SARS-CoV-2 RBD, crystal structures of this domain in complex with the cellular receptor protein ACE2 was reported by 24 and by Yan et al. 25 . Of note, one predicted interaction region almost completely overlaps with the substructure of spike protein RDB engaged in binding with ACE2 (478 TPCNGVEGF 486). Synthetic mimicry of this sequence could aptly generate high priority candidates aimed at disrup.....
Document: Importantly, after we ran our predictions on the SARS-CoV-2 RBD, crystal structures of this domain in complex with the cellular receptor protein ACE2 was reported by 24 and by Yan et al. 25 . Of note, one predicted interaction region almost completely overlaps with the substructure of spike protein RDB engaged in binding with ACE2 (478 TPCNGVEGF 486). Synthetic mimicry of this sequence could aptly generate high priority candidates aimed at disrupting PPIs between SARS-CoV-2 RBD and its cell receptor ACE2. Such molecules could be used to block viral entry into cells.
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