The ‘D614G’ mutation (Aspartate-to-Glycine change at position 614) of the SARS-CoV-2 spike protein has been speculated to adversely affect the efficacy of most vaccines and countermeasures that target this glycoprotein, necessitating frequent vaccine matching. Virus neutralisation assays were performed using sera from ferrets which received two doses of the INO-4800 COVID-19 vaccine, and Australian virus isolates (VIC01, SA01 and VIC31) which either possess or lack this mutation but are otherwise comparable. Through this approach, supported by biomolecular modelling of this mutation and the commonly-associated P314L mutation in the RNA-dependent RNA polymerase, we have shown that there is no experimental evidence to support this speculation. We additionally demonstrate that the putative elastase cleavage site introduced by the D614G mutation is unlikely to be accessible to proteases.
【저자키워드】 SARS-CoV-2, Vaccines, viral evolution, 【초록키워드】 Efficacy, Vaccine, COVID-19 vaccine, Mutation, Spike protein, D614G mutation, virus isolate, ferret, sera, RNA-dependent RNA polymerase, glycoprotein, Proteases, neutralisation assay, dose, INO-4800, Support, cleavage site, experimental evidence, Affect, approach, shown, performed, lack, unlikely, supported, introduced, comparable, the SARS-CoV-2, 【제목키워드】 Vaccine, in silico, D614G mutation, SARS-CoV-2 spike protein, Evidence, affected, unlikely,