Differential Tropism of SARS-CoV and SARS-CoV-2 in Bat Cells
Susanna K.P. Lau
1 , Antonio C.P. Wong
1, Hayes K.H. Luk
1, Kenneth S.M. Li, Joshua Fung, Zirong He, Flora K.K. Cheng, Tony T.Y. Chan, Stella Chu, Kam Leng Aw-Yong, Terrence C.K. Lau, Kitty S.C. Fung, and Patrick C.Y. Woo
Author affiliations: The University of Hong Kong, Hong Kong, China (S.K.P. Lau, A.C.P. Wong, H.K.K. Luk, K.S.M. Li, J. Fung, Z. He, F.K.K. Cheng, T.T.Y. Chan, S. Chu, K.L. Aw-Yong, P.C.Y. Woo); City University of Hong Kong, Hong Kong (T.C.K. Lau); United Christian Hospital, Kwun Tong, Hong Kong (K.S.C. Fung)
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Figure 2
Figure 2. Structural modeling of the human (A, D), Rhinolophus sinicus bat (Rs-bat) (B, E), and Pipistrellus abramus bat (Pa-bat) (C, F) ACE2 with the receptor-binding domain (RBD) of the spike proteins of SARS-CoV and SARS-CoV-2. The models of RBDs of SARS-CoV and SARS-CoV-2 (yellow) are shown with human (purple), Rs-bat (pink). and Pa-bat (green) ACE2 structures in ribbon diagrams. The interface of different RBDs and human/bat ACE2 are shown and the residues with potential impact on binding affinity are shown in ball-and-stick format. Images were produced using Discovery Studio visualizer (Accelrys, https://www.accelrys.com).
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