Key result
The D614G mutation in the SARS-CoV-2 S-glycoprotein demonstrated a higher binding affinity for furin (-61.9 kcal/mol) compared to the wild type (-56.78 kcal/mol), suggesting increased viral infectivity.
The D614G mutation in SARS-CoV-2 increases the binding affinity of furin to the S-glycoprotein, likely enhancing viral infectivity and transmission.
May guide SARS-CoV-2 variant surveillance; leaves open furin as a therapeutic target.
COVID-19 pandemic has inflicted serious challenges to both global health and economy. The disease is caused by a +ssRNA zoonotic coronavirus named SARS-CoV-2, known to have four structural proteins named spike (S), envelope (E), membrane (M), and nucleocapsid (N)
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Sindhu et al. (2021) conducted a review in COVID-19 (SARS-CoV-2). D614G mutation in SARS-CoV-2 S-glycoprotein vs. D614 wild type S-glycoprotein was evaluated on Furin binding free energy (kcal/mol). The D614G mutation in the SARS-CoV-2 S-glycoprotein demonstrated a higher binding affinity for furin (-61.9 kcal/mol) compared to the wild type (-56.78 kcal/mol), suggesting increased viral infectivity.
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