Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2

Corresponding author: Jinghua Yan, Jianxun Qi

Affiliation: University of the Chinese Academy of Sciences

Publication date: this article was published online on May 14, 2020

DOI: https://doi.org/10.1016/j.cell.2020.03.045

Highlights

The researchers present the crystal structure of the C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike (S) protein in complex with human ACE2 (hACE2), which reveals a hACE2-binding mode similar overall to that observed for SARS-CoV. However, atomic details at the binding interface demonstrate that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-RBD. Additionally, a panel of murine monoclonal antibodies (mAbs) and polyclonal antibodies (pAbs) against SARS-CoV-S1/receptor-binding domain (RBD) were unable to interact with the SARS-CoV-2 S protein, indicating notable differences in antigenicity between SARS-CoV and SARS-CoV-2.

Nomination Reason

This work sheds light on the viral pathogenesis and provide important structural information regarding development of therapeutic countermeasures against the emerging virus.

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