Fig. 7: In silico and in vitro assessment of the hACE2 receptor binding potential of a potentially zoonotic SARS-related coronavirus. | Nature Communications

Fig. 7: In silico and in vitro assessment of the hACE2 receptor binding potential of a potentially zoonotic SARS-related coronavirus.

From: Individual bat virome analysis reveals co-infection and spillover among bats and virus zoonotic potential

Fig. 7

a Top, homology-modeling structure of the receptor-binding ___domain (RBD) of Bat SARS-like coronavirus CX1 in complex with human angiotensin-converting enzyme 2 (hACE2). Blue-colored residues on RBD indicate amino acid differences compared with SARS-CoV-2 Wuhan-Hu-1. Bottom, alignment of RBD sequences (residues T333 to G526 of spike protein) of Bat SARS-like coronavirus CX1, SARS-CoV-2 Wuhan-Hu-1 and two closely related bat coronavirus. Only polymorphic sites are shown. The five amino acid differences in the RBD of Bat SARS-like coronavirus CX1 compared to SARS-CoV-2 Wuhan-Hu-1 are marked with blue dots. b Molecular dynamics simulation results of binding energy  (top) and binding stability (bottom) of Bat SARS-like coronavirus CX1 RBD-hACE2 complex. c The binding capability of SARS-CoV, SARS-CoV-2 and Bat SARS-like coronavirus CX1 RBD proteins to hACE2 protein was tested with various concentrations of the RBD proteins via ELISA. d The binding kinetics was determined by the biolayer interferometry (BLI) binding analysis. The purified hACE2 were coated on the sensor followed by the injection of various concentrations of SARS-CoV, SARS-CoV-2 and Bat SARS-like coronavirus CX1 RBD proteins. Source data are provided as a Source Data file.

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