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- Letters to the EditorOpen Access
Noneffect of SARS-CoV-2 spike glycoprotein Y217N mutation on affinity between the virus and ACE2
Journal of Biological ChemistryVol. 296100725Published online: May 27, 2021- Takuma Hayashi
- Ikuo Konishi
Cited in Scopus: 0The interaction between the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and angiotensin-converting enzyme 2 (ACE2), the primary entry receptor for SARS-CoV-2, is a key determinant of the range of hosts that can be infected by the virus. Zhang et al. (1) reportedly constructed human ACE2 (hACE2) with the Y217N mutation and found that this mutation completely blocked SARS-CoV-2 entry. Zhang et al. (1) performed an receptor binding domain (RBD) binding assay and found that WT hACE2 potently bound the RBD; however, hACE2 Y217N almost lost the ability to bind the RBD.