Sisi Shan

TL;DR: High-resolution crystal structures of the receptor-binding domain of the spike protein of SARS-CoV-2 and SARS -CoV in complex with ACE2 provide insights into the binding mode of these coronaviruses and highlight essential ACE2-interacting residues.

TL;DR: In a study of antibodies isolated from patients infected with SARS-CoV-2, antibodies that potently neutralized the virus competed with angiotensin-converting enzyme 2 for binding to the receptor-binding domain of the viral spike protein, suggesting that antibodies that disrupt this interaction could be developed to treat Sars-Cov-2 infection.

TL;DR: Results suggest that antibody response to RBDs is viral species-specific while that cross-recognition target regions outside the RBD are cross- Recognition target areas outside the SARS-CoV-2.

TL;DR: The crystal structure of the 2019-nCoV spike receptor-binding domain (RBD) bound with the cell receptor ACE2 is determined, and similarity in structure and sequence strongly argue for a convergent evolution between 2019- nCoV and SARS-CoV RBD for improved binding to ACE2 despite of being segregated in different genetic lineages in the betacoronavirus genus.

TL;DR: In this paper, the top three most potent yet variable neutralizing antibodies for SARS-CoV-2 infection in Ad5-hACE2-sensitized mice were identified.