The infectiousness of the variant is in part determined by the 37 mutations in the amino acid sequences of its spike protein that distinguish it from the virus strain discovered in Wuhan.
These mutations have been shown to help the variant evade antibodies generated by the six most commonly used vaccines, and all but one of monoclonal antibodies used to counter infections.
As the mutations also affect the structure of the region of the spike protein responsible for attaching to and entering cells, a tradeoff had been expected where they might simultaneously restrict the variant’s ability to bind to target cells.
The new study used cryo-electron microscopic and X-ray crystallographic studies to get an extremely detailed view of the omicron spike protein and reveal that the proposed tradeoff does not apply to it.
The mutations do indeed change how the protein interacts with antibodies so that the ability of almost all monoclonal antibodies against it is reduced, but, at the same time, the ability of the spike’s receptor-binding domain to bind to human cells at the ACE2 receptor is actually enhanced, so it is able bind to even more tightly.
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