The S protein sequences of both the RaTG13 and SARS-CoV-2 were 97.8% conservative in the ectodomain. However, 89.6% of the sequence in the receptor-binding domain (RBD) varied, with substitutions in the ACE2-receptor-binding surface and the RBD–RBD interfaces of the trimeric S.

University of Michigan - Ann Arbor

- Cry-electron microscopy (cryo-EM) structures of S glycoprotein of bat virus RaTG13 and uncleaved SARS-CoV-2
- S glycoprotein sequences of RaTG13 and SARS-CoV-2
- S glycoprotein stability 
- Bat virus RaTG13 and SARS-CoV-2 S glycoprotein affinities to human receptor ACE2

Comparison of S glycoprotein between RaTG13 and uncleaved SARS-CoV-2

Wrobel, A.G., Benton, D.J., Xu, P. et al. SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects. Nat Struct Mol Biol (2020). https://doi.org/10.1038/s41594-020-0468-7

SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects

Cry-electron microscopy (cryo-EM) structures of S glycoprotein of bat virus RaTG13 and an uncleaved SARS-CoV-2 were created. The structure of the S glycoprotein in RaTG13 is shown to be very similar to that of the closed form of uncleaved SARS-CoV-2.

Cry-electron microscopy (cryo-EM) structures of S glycoprotein of bat virus RaTG13 and uncleaved SARS-CoV-2

S glycoprotein sequences of RaTG13 and SARS-CoV-2

Using thermal-stability data, it was concluded that the uncleaved SARS-CoV-2 S protein had higher stability than RaTG13 S protein and cleaved SARS-CoV-2 had similar stability to uncleaved RaTG13 protein. 

S glycoprotein stability

Amplitude analysis provides evidence that SARS-CoV-2 binds more tightly to human ACE2 than the bat virus protein does by around 1,000 times. 

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