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. 2022 Jun 15;27(12):3851. doi: 10.3390/molecules27123851

Figure 2.

Figure 2

How the D614G mutation and the ADE antibody 1052 enhance SARS-CoV-2 infectivity. (A) Hydrogen bond between D614 (chain B) and T859 (chain C) stabilizing the trimeric spike protein (PDB: 6VSB). (B) The D614G mutation renders impossible the formation of the hydrogen bond and facilitates the conformational change inducing the demasking of the RBD (PDB: 7BNM). (C) Binding of ADE antibody 1052 breaks the hydrogen bond between D614 and T859 (PDB: 7LAB). The arrow in panels B and C illustrates the lack of contact between vicinal spike protein monomers in the context of the trimeric association.