Structural basis of receptor recognition by SARS-CoV-2

Corresponding author: Fang Li

Affiliations: Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, MN, USA; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, USA.

Publication date: this article was published online on March 30, 2020

DOI: https://doi.org/10.1038/s41586-020-2179-y

Highlights

The researchers determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 (engineered to facilitate crystallization) in complex with ACE2. In comparison with the SARS-CoV RBD, they observed that an ACE2-binding ridge in SARS-CoV-2 RBD has a more compact conformation; moreover, several residue changes in the SARS-CoV-2 RBD stabilize two virus-binding hotspots at the RBD–ACE2 interface. They also demonstrated that these structural features of SARS-CoV-2 RBD increase its ACE2-binding affinity. Additionally, they showed that RaTG13, a bat coronavirus that is closely related to SARS-CoV-2, also uses human ACE2 as its receptor. 

Nomination Reasons

The authors revealed the differences among SARS-CoV-2, SARS-CoV and RaTG13 in ACE2 recognition, which should shed light on the potential animal-to-human transmission of SARS-CoV-2. This study also provides guidance for intervention strategies that target receptor recognition by SARS-CoV-2.

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