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Coronaviruses with a SARS-CoV-2-like receptor-binding domain allowing ACE2-mediated entry into human cells isolated from bats of Indochinese peninsula

Authors
Temmam S, Vongphayloth K, Salazar EB, Munier S, Bonomi M, Régnault B, Douangboubpha B, Karami Y, Chretien D, Sanamxay D, Xayaphet V, Paphaphanh P, Lacoste V, Somlor S, Lakeomany K, Phommavanh N, Pérot P, Donati F, Bigot T, Nilges M, Rey F, Werf Svd, Brey P, Eloit M.
Year
2021
DOI
10.21203/rs.3.rs-871965/v1
Source
europepmc
Original
https://www.researchsquare.com/article/rs-871965/latest.pdf
Record id
tt:5Av3q_Yyc2jvYadPTn2w3vgwMPBgyaT4N27DtBCwiSc
Payload sha256
41a0e6b88987e5d6ec21d849eb9d50f80750025ebdf88842e0ef1c7e4f94e722

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References

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  61. A) Biolayer interferometry binding analysis of the hACE2 peptidase domain to immobilized BANAL52/103 or BANAL-236 RBDs. Black lines correspond to global t of the data using a 1:1 binding model. (B) Frequency of formation of salt bridges at the interface of RBD and hACE2 during the course of the MD simulations. The analysis is performed for 9 different MD simulations (3 replicates for each complex) of hACE2 in complex with SARS-CoV-2 (shades of green), BANAL-236 (shades of red) and BANAL-52/103 RBDs (shades of blue). (C) Ribbon representations of the crystal structures of hACE2 peptidase domain (cyan) in complex with SARS-CoV-2 (PDB 6M0J) or BANAL-236 (this study, PDB 7PKI)
  62. RBDs (pink). Black arrows in the overall structures indicate the structural difference between the two complexes at the level of helix H4. The insets show the main interactions in the ACE2-RBD interfaces. Residues in the RBM mutated between SARS-CoV-2 and BANAL-236 are indicated with colored boxes.