A recent study from the Pasteur Institute, Temmam et al., investigates viruses endemic to the bats of Southeast Asia and found close relatives of SARS-CoV-2 among them.
The original SARS-CoV-2 Wuhan strain has 17 amino acid contact points between the virus and the ACE2 receptor.
The authors conducted several experiments to determine whether similarity in the receptor-binding domain region of the Spike protein of the BANAL-20-52, 103, and 236 translated to a similar function to that of SARS-CoV-2. Their first question was whether the receptor-binding domain of the viruses is capable of infecting cells that carry the human ACE2 receptor. Using a pseudotype virus on cells in culture, they found that the answer is a resounding yes.
Finally, to analyze the binding structure, they used x-ray crystallography at 2.9-angstrom resolution for both SARS-CoV-2 and BANAL-20-52. The figure below displays the structural similarities and differences between the two complexes, particularly the mutated residues in the receptor-binding domain and the structural complexes in the helices. As expected, most of the interactions observed between the ACE2 and SARS-CoV-2 receptor-binding domain were also present for BANAL-236.
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