Short Communication Open Access
Volume 3 | Issue 3 | DOI: https://doi.org/10.33696/immunology.3.095

Increased Binding Affinity of Furin to D614G Mutant S-glycoprotein May Augment Infectivity of the Predominating SARS-CoV-2 Variant

  • 1Animal & Imaging core facility, Dasman Diabetes Institute, Kuwait
  • 2Department of Immunology & Microbiology, Dasman Diabetes Institute, Kuwait
  • 3Department of Genetics & Bioinformatics, Dasman Diabetes Institute, Kuwait
+ Affiliations - Affiliations

Corresponding Author

Fahd Al-Mulla, fahd.almulla@dasmaninstitute.org ;
Sardar Sindhu, sardar.sindhu@dasmaninstitute.org

Received Date: January 24, 2021

Accepted Date: May 07, 2021


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

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