Fig. 4: The effects of the SP of SARS-CoV-2 on the crosstalk between ACE and ACE2.
From: Protein nanopore reveals the renin–angiotensin system crosstalk with single-amino-acid resolution
a, Illustration of the binding between the SARS-CoV-2 SP and ACE2 (PDB 6M0J). b, Time-dependent probability of Ang peptides during the cleavage of Ang I by ACE2 and ACE without (left) and with (right) the SP of SARS-CoV-2, respectively. c, Illustration of Ang I metabolism pathways regulated by ACE and ACE2. d,e, Time-dependent cleavage quantity of ACE2 (d) or ACE (e), and the corresponding inhibition or enhancement (open circles) induced by SARS-CoV-2 SP. f, Mutation sites in the SP of the SARS-CoV-2 Delta variant. g, Time-dependent probability of Ang peptides during the cleavage of Ang I by ACE2 and ACE with Delta SP. h, Enhancement of Ang II accumulated and produced by the Delta SP compared to SP. The data were acquired in 1.0 M KCl with 10 mM HEPES and 10 μM ZnCl2 at pH 8.0 under an applied potential of +140 mV. The concentrations of ACE and ACE2 were 36 nM and 1.2 nM, respectively, with 17 nM SP of SARS-CoV-2 or SARS-CoV-2 Delta variant, and an initial Ang I substrate concentration of 13.1 μM. The reaction temperature was set to 21 ± 1 °C.
