The SARS-CoV-2 exerts a distinctive strategy for interacting with the ACE2 human receptor


The COVID-19 disease has plagued over 110 countries and has resulted in over 4,000 deaths within 10 weeks. We compare the interaction between the human ACE2 receptor and the SARS-CoV-2 spike protein with that of other pathogenic coronaviruses using molecular dynamics simulations. SARS-CoV, SARS-CoV-2, and HCoV-NL63 recognize ACE2 as the natural receptor but present a distinct binding interface to ACE2 and a different network of residue-residue contacts. SARS-CoV and SARS-CoV-2 have comparable binding affinities achieved by balancing energetics and dynamics. The SARS-CoV-2–ACE2 complex contains a higher number of contacts, a larger interface area, and decreased interface residue fluctuations relative to SARS-CoV. These findings expose an exceptional evolutionary exploration exerted by coronaviruses toward host recognition. We postulate that the versatility of cell receptor binding strategies has immediate implications on therapeutic strategies.


DOI: 10.1101/2020.03.10.986398

Projects: COVID-19 Disease Map

Publication type: Tech report

Citation: biorxiv;2020.03.10.986398v1,[Preprint]

Date Published: 12th Mar 2020


Registered Mode: imported from a bibtex file

Authors: Esther S. Brielle, Dina Schneidman-Duhovny, Michal Linial

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Brielle, E. S., Schneidman-Duhovny, D., & Linial, M. (2020, March 12). The SARS-CoV-2 exerts a distinctive strategy for interacting with the ACE2 human receptor. []. Cold Spring Harbor Laboratory.

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Created: 8th Apr 2020 at 22:13

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