The analysis conducted by the researchers found how the virus evolved to increase transmissibility and elusiveness
Omicron Spike Protein features 37 unpublished mutations, a number that is three to five times higher than that observed in the previous variants. The structural analysis, carried out thanks to cryoelectronic microscopy, indicates that different mutations (R493, S496 and R498) give rise to new ionic bonds and hydrogen bonds between the Spike and the Ace-2 receptor. These ties they increase the affinity of the virus for human cells, while other mutations (such as K417N) reduce the strength of these bonds.
“Overall, these results indicate that Omicron has a higher binding affinity compared to the original virus, with levels more similar to what we see with the Delta variant, “explains the study coordinator, Sriram Subramaniam.” It should be noted how the Omicron variant si evolved to retain its ability to bind to human cells despite such a large number of mutations “.
Further experiments show that Omicron has an ability to evade antibodies that is greater than the previous variants: it manages to evade all six monoclonals tested (five of which are completely ineffective), while showing an increased ability to evade antibodies produced by people vaccinated or cured of Covid-19. “In particular, Omicron escapes less vaccine-induced immunity compared to that generated by natural infection in unvaccinated patients. This – concludes the biochemist Subramaniam – suggests that vaccination remains one of our best defense weapons“.