Spike protein mutations in Omicron subvariants increase their susceptibility to reductive cleavage of disulfide bonds UofT biorxivpreprint SARSCoV2 COVID19 Omicron SpikeProtein Mutation
By Dr. Chinta SidharthanJan 10 2023Reviewed by Aimee Molineux In a recent study posted to the bioRxiv* preprint server, researchers discovered that the spike protein of severe acute respiratory syndrome coronavirus 2 is susceptible to cleavage at the disulfide bonds. They also found that the vulnerability to reductive cleavage varies across variants, with the Omicron variant family being highly susceptible to reduction.
About the study In the present study, the researchers used a tri-part Nanoluciferase assay to measure the change in the spike protein-ACE2 binding after the reductive cleavage of the spike protein disulfide bonds. Compared to traditionally used methods for binding affinity measurement, such as surface plasmon resonance, the tNLuc assay is cost-effective and does not require complicated equipment.
The mutations in the RBM of the Omicron variants were examined to determine those that make the Omicron subvariants more vulnerable to disulfide reduction than earlier strains. Loss- and gain-of-function approaches were used to determine the roles of the identified mutations. Furthermore, the specific disulfide bonds in the Omicron RBD that undergo reductive cleavage were also identified using chemical-labeled mass spectrometry.
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