Science Announces Molecular-Level Analysis of World's First Omicron Spike Protein

"Understanding the molecular structure of the viral spike protein is important as it can help us develop more effective therapeutic Omicron and related variants in the future," said lead author Sriram Subramaniam, Ph.

The spike protein located on the outside of the coronavirus enables SARS-CoV-2 to enter human cells

Structural analysis revealed that some mutations (R493, S496 and R498) established new salt bridges and hydrogen bonds between the spike protein and the human cell receptor ACE2

Dr Subramaniam said: "Overall, the findings suggest that Omicron has greater binding affinity than the original virus, at levels more similar to what we have seen with the Delta virus variant

The researchers conducted further experiments showing that the Omicron spike protein exhibited increased antibody evasion

Notably, Omicron evaded less immunity from vaccines than immunity from natural infection in unvaccinated patients

As a next step, Dr.

"An important focus of our team is to better understand the binding of neutralizing antibodies, as well as therapeutics that are effective across the full spectrum of variants, and how these approaches can be used to develop anti-variant therapies

article title

SARS-CoV-2 Omicron Variant: ACE2 Binding, Cryo-EM Structure of Spike Protein-ACE2 Complex and Antibody Evasion