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

Abstract

The coronavirus disease (COVID)-19 pandemic has profoundly devastated human health and wellbeing all over the world, along with colossal setback to global economy in terms of soaring new infections, hospitalizations, ICU admissions, work losses, closures of businesses and institutions, bankruptcies, and precautionary measures involving social distancing, hygiene, and travel restrictions across the globe. COVID-19 was declared by the World Health Organization (WHO) as a public health emergency of international concern in January 2020, and then as a pandemic in March 2020. There are over 154.64 million confirmed coronavirus infections and more than 3.23 million deaths reported to the WHO globally until date (as of 11:21 a.m. CEST, 6 May, 2021) [1]. The disease is caused by a zoonotic positive-sense single-stranded ssRNA virus called severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which is known to have four structural proteins: spike (S), envelope (E), membrane (M), and nucleocapsid (N), with close genetic similarity to bat coronaviruses. The global science initiative source called “Global Initiative on Sharing Avian Influenza Data” (GISAID) has reported seven SARS-CoV-2 clades as G, GH, GR, L, O, S, and V [2].