Scientists from the University of British Columbia School of Medicine have performed the world’s first structural analysis of the spike omicron protein at the molecular level. Work revealed how strong the mutation Variant of Omikron It attaches to and infects human cells. The research was carried out using an electron microscope.
Spinal protein of the Omikron . variant
The bumps on the outer surface of SARS-CoV-2 allow it to penetrate human cells. His Omikron variant 37 additional boom In the spiny protein – three to five times more than in the previous variants.
Structural analysis showed that several of the mutants (R493, S496, and R498) form new salt bonds and hydrogen bonds between the spiny protein and the human cell receptor known as ACE2. The researchers conclude that these new links appear to increase the strength of the virus’s attachment to human cells – while the other mutations (K417N) decrease the strength of this link. Other experiments showed that omicron protein increases antibody avoidance.
It is noteworthy that Omicron avoided immunity caused by vaccines to a lesser degree than resistance to natural infections in unvaccinated patients. This indicates that vaccination remains our best defense against the virus, said lead author Dr Sriram Subramaniam, professor in the Department of Biochemistry and Molecular Biology.
Based on the observed increase in binding affinity, the scientists concluded Elevated protein mutations are likely to be contributing factors to the increased transmission of the Omikron variant.
The research team will use this knowledge to support the development of more effective treatments. Dr. Sriram Subramaniam added: “Understanding the molecular structure of the viral spinal protein is important to allow us to develop more effective therapies against Omicron and related variants in the future.”
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