Increased elastase sensitivity and decreased intramolecular interactions in the more transmissible 501Y.V1 and 501Y.V2 SARS-CoV-2 variants' spike protein-an in silico analysis

Two SARS-CoV-2 variants of concern showing increased transmissibility relative to the Wuhan virus have recently been identified. Although neither variant appears to cause more severe illness nor increased risk of death, the faster spread of the virus is a major threat. Using computational tools, we found that the new SARS-CoV-2 variants may acquire an increased transmissibility by increasing the propensity of its spike protein to expose the receptor binding domain via proteolysis, perhaps by neutrophil elastase and/or via reduced intramolecular interactions that contribute to the stability of the closed conformation of spike protein. This information leads to the identification of potential treatments to avert the imminent threat of these more transmittable SARS-CoV-2 variants.

Automated summary

Two SARS-CoV-2 variants of concern have been identified recently, showing increased transmissibility compared to the Wuhan virus. While these variants do not appear to cause more severe illness or increased risk of death, the faster spread of the virus poses a major threat. Computational tools suggest that the increased transmissibility of the new variants may be due to changes in the spike protein structure, which could help in identifying potential treatments to combat these more transmittable strains.