Omicron, the Most Structurally Stable Variant of COVID-19... Potential Increase in Transmissibility

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[Asia Economy Reporter Kim Young-won] A study has found that the COVID-19 virus is evolving in a way that increases cell binding affinity, thereby enhancing its transmissibility.

On the 12th, the Korea Disease Control and Prevention Agency (KDCA), in collaboration with Professor Kang Nam-sook's research team at Chungnam National University, announced the results of an analysis of the spike protein structures of domestic COVID-19 variants including Omicron, Alpha, Delta, Mu, and D614G.

According to the study, Omicron exhibited the lowest variance in the distances among the three spike protein subunits, forming the most stable structure. Following Omicron, the order of stability was Delta, Mu, Alpha, and the non-variant virus.

The KDCA explained that COVID-19 is evolving to increase binding affinity by enhancing structural stability during cell infection, and that variants with superior structural stability are likely to emerge in the future.

Kim Eun-jin, head of the testing and analysis team at the Central Disease Control Headquarters, stated, "Higher structural stability means an increased likelihood of binding between the virus and cells," adding, "As COVID-19 evolves through mutations, the structural stability of the spike protein that binds to cells has gradually increased, which likely led to increased binding affinity and consequently higher transmissibility."

The results of this analysis are scheduled to be published in the latest issue of the International Journal of Molecular Sciences.

This content was produced with the assistance of AI translation services.