Análise in silico da interação entre proteínas spike de novas variantes de SARS-CoV-2 e isoformas da enzima conversora de angiotensina 2

Abstract

The novel SARS-CoV-2 coronavirus that is responsible for the COVID-19 pandemic presents worrying severity, high transmission and high mutation rate, and therefore, the SARS-CoV-2 spike protein, which mediates virus entry into the cell, and its interaction with the human cellular receptor ECA2 have become targets of studies. In this context, molecular features intrinsic to the SARS-CoV-2 spike protein and ECA2 interaction that potentially account for changes in the transmissibility rate, severity, and impact on the immune system of SARS-CoV-2 variants are sought. To this end, in silico protein-protein interaction analyses have proven to be efficient methodologies for rapid scientific conclusions about this interaction. It was found that in the intermolecular interaction between the SARS-CoV-2 spike protein and ECA2 the residues Arg403 in the original Wuhan structure, Arg498 and Arg403 in the Omicron variant and Lys440, His505, Arg403 and Arg498 in the BA.2 subvariant that left the interactive surface profile of the spike more positive. This suggests positive selection promoting greater stability in charge attraction binding, as the ECA2 surface has a predominantly electronegative profile.