Open AccessIncreased 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
Author(s) -
Suman Pokhrel,
Benjamin R. Kraemer,
Lucia Lee,
Kate Samardzic,
Daria MochlyRosen
Publication year - 2021
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0251426
Subject(s) - transmissibility (structural dynamics) , spike protein , in silico , spike (software development) , proteolysis , covid-19 , biology , computational biology , genetics , medicine , disease , biochemistry , gene , computer science , enzyme , physics , software engineering , vibration isolation , quantum mechanics , infectious disease (medical specialty) , vibration
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.