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). Given the critical role in host immunity and virus attachment to ACE2 receptors on target cells, S-glycoprotein mutations are of significant concern. Dynamic tracking and phylogenetic analysis show that S-glycoprotein variants of SARS-CoV-2 (G clade) are emerging globally, particularly the D614G S-glycoprotein variant has been fast spreading through human transmissions in all over Europe since March 2020. Herein, we review a recently published study which characterizes the D614G mutation in SARS-CoV-2 S-glycoprotein and deciphers its impact on furin binding and viral infectivity using bioinformatics tools and molecular dynamic simulations. The findings of this study are reviewed in light of evidence from other studies. In the end, consistent need for epidemiological tracking of other S-glycoprotein variants as well as future perspectives have been addressed.

COVID-19, SARS-CoV-2, D614G, S-glycoprotein, Furin, ACE2, Infectivity