Author: Cheng Wang; Shaobo Wang; Daixi Li; Xia Zhao; Songling Han; Tao Wang; Gaomei Zhao; Yin Chen; Fang Chen; Jianqi Zhao; Liting Wang; Wei Sun; Yi Huang; Yongping Su; Dongqing Wei; Jinghong Zhao; Junping Wang
Title: Lectin-like Intestinal Defensin Inhibits 2019-nCoV Spike binding to ACE2 Document date: 2020_3_31
ID: bzq1xxqb_14
Snippet: The interaction between 2019-nCoV S1 and ACE2 was measured as well. The purified S1 expressed by human HEK293 cells intensively bound ACE2 with an affinity of 2.68 nM ( Figure 1D ). This assay conforms to the fact that virus forwardly contact ACE2 located on the cell surface and may avoid the steric hindrance of a receptor binding to its ligand. We reversely loaded S1 and measured the recruitment of ACE2. As shown in Figure S1 , the binding thick.....
Document: The interaction between 2019-nCoV S1 and ACE2 was measured as well. The purified S1 expressed by human HEK293 cells intensively bound ACE2 with an affinity of 2.68 nM ( Figure 1D ). This assay conforms to the fact that virus forwardly contact ACE2 located on the cell surface and may avoid the steric hindrance of a receptor binding to its ligand. We reversely loaded S1 and measured the recruitment of ACE2. As shown in Figure S1 , the binding thickness was low, whereas the affinity (3.8 nM) was comparable to that of S1 binding to ACE2. Also, we noticed that the S1-ACE2 affinity was higher than those of S-ACE2 and RBD-ACE2 interactions 15, 32 . The discrepancy may be attributed to different proteins employed in different experiments.
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