tetano
Editor, Senior Moderator
Nature. 2020 Mar 30. doi: 10.1038/s41586-020-2180-5. [Epub ahead of print]
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor.
Lan J[SUP]1[/SUP], Ge J[SUP]1[/SUP], Yu J[SUP]1[/SUP], Shan S[SUP]2[/SUP], Zhou H[SUP]3[/SUP], Fan S[SUP]1[/SUP], Zhang Q[SUP]2[/SUP], Shi X[SUP]2[/SUP], Wang Q[SUP]3[/SUP], Zhang L[SUP]4[/SUP], Wang X[SUP]5[/SUP].
Author information
Abstract
A novel and highly pathogenic coronavirus (SARS-CoV-2) has caused an outbreak in Wuhan city, Hubei province of China since December 2019, and soon spread nationwide and spilled over to other countries around the world[SUP]1-3[/SUP]. To better understand the initial step of infection at an atomic level, we determined the crystal structure of the SARS-CoV-2 spike receptor-binding domain (RBD) bound to the cell receptor ACE2 at 2.45 ? resolution. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also utilizes ACE2 as the cell receptor[SUP]4[/SUP]. Structural analysis identified residues in the SARS-CoV-2 RBD that are critical for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly argue for convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses[SUP]1-3,5[/SUP]. The epitopes of two SARS-CoV antibodies targeting the RBD are also analysed with the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies.
PMID:32225176DOI:10.1038/s41586-020-2180-5
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor.
Lan J[SUP]1[/SUP], Ge J[SUP]1[/SUP], Yu J[SUP]1[/SUP], Shan S[SUP]2[/SUP], Zhou H[SUP]3[/SUP], Fan S[SUP]1[/SUP], Zhang Q[SUP]2[/SUP], Shi X[SUP]2[/SUP], Wang Q[SUP]3[/SUP], Zhang L[SUP]4[/SUP], Wang X[SUP]5[/SUP].
Author information
Abstract
A novel and highly pathogenic coronavirus (SARS-CoV-2) has caused an outbreak in Wuhan city, Hubei province of China since December 2019, and soon spread nationwide and spilled over to other countries around the world[SUP]1-3[/SUP]. To better understand the initial step of infection at an atomic level, we determined the crystal structure of the SARS-CoV-2 spike receptor-binding domain (RBD) bound to the cell receptor ACE2 at 2.45 ? resolution. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also utilizes ACE2 as the cell receptor[SUP]4[/SUP]. Structural analysis identified residues in the SARS-CoV-2 RBD that are critical for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly argue for convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses[SUP]1-3,5[/SUP]. The epitopes of two SARS-CoV antibodies targeting the RBD are also analysed with the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies.
PMID:32225176DOI:10.1038/s41586-020-2180-5