Fig. 3: Cryo-EM structures of NeoCoV RBD and PDF-2180 RBD in a complex with Bat37ACE2.
From: Close relatives of MERS-CoV in bats use ACE2 as their functional receptors
a,b, Cryo-EM density map (left) and ribbon representation (right) of the NeoCoV RBD–Bat37ACE2 complex (a) and the PDF-2180 RBD–Bat37ACE2 complex (b). NeoCoV RBD, PDF-2180 RBD and Bat37ACE2 are coloured red, orange and cyan, respectively. c, Structural comparison between the NeoCoV RBD–Bat37ACE2 complex (left, PDB: 7WPO) and MERS-CoV RBD-hDPP4 complex (right, PDB: 4KR0). The NeoCoV RBD, MERS-CoV RBD, NeoCoV RBM, MERS-CoV RBM, Bat37ACE2 and hDPP4 are coloured red, green, yellow, grey, cyan and purple, respectively. d, Magnified view of the NeoCoV RBD–Bat37ACE2 complex interface. All of the structures are shown as ribbon representations with key residues rendered as sticks. Salt bridges and hydrogen bonds are shown as red and yellow dashed lines, respectively. e–g, The contribution of critical NeoCoV RBD residues to receptor binding (e) and pseudotyped virus entry (f) in HEK293T-Bat37ACE2 cells. g, The effect of mutations on S expression (lysate) and virion incorporation (supernatant) in HEK293T cells. h–j, The contribution of critical Bat37ACE2 residues on NeoCoV RBD binding (h), pseudotyped virus entry (i) and the impact of mutations on ACE2 expression (j) in HEK293T cells. For e–j, data are representative of two independent infections assays. Two independent preparations of pseudoviruses were used for the assays shown in e–g. Data are mean ± s.d. for f (biological triplicates of infected cells) and i (biological quadruples of infected cells). Statistical analysis was performed using two-tailed unpaired Student’s t-tests. For e and h, scale bars, 100 μm.
