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. 2020 Dec 10;183(6):1732. doi: 10.1016/j.cell.2020.11.031

Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion

Alexandra C Walls, Xiaoli Xiong, Young-Jun Park, M Alejandra Tortorici, Joost Snijder, Joel Quispe, Elisabetta Cameroni, Robin Gopal, Mian Dai, Antonio Lanzavecchia, Maria Zambon, Félix A Rey, Davide Corti, David Veesler
PMCID: PMC7834669  PMID: 33306956

(Cell 176, 1026–1039.e1–e15; February 21, 2019)

We recently discovered that the purified ACE2 ectodomain used in the manuscript encompasses residues 19–741 of macaque ACE2 instead of residues 1–615 of human ACE2. Although the binding interface is conserved, the presence of the endogenous ACE2 dimerization domain affects the affinities reported in Figure S7 due to avidity. New measurements were carried out with the human ACE2 ectodomain (residues 19–615), and the corresponding binding affinities for the RBD were corrected (Starr, T.N., et al. (2020). Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding. Cell 182, 1295–1310. 10.1016/j.cell.2020.08.012). Our conclusions remain unchanged. We apologize for any confusion that this error may have caused.


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