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bioRxiv · 10.1101/2023.02.10.528025

Positing changes in neutralizing antibody activity for SARS-CoV-2 XBB.1.5 using in silico protein modeling

Ford, C. T.·Yasa, S.·Jacob Machado, D. T.·White, R. A.·Janies, D. A.
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Abstract

The SARS-CoV-2 variant XBB.1.5 is of concern as it has high transmissibility. XBB.1.5 currently accounts for upwards of 30% of new infections in the United States. One year after our group published the predicted structure of the Omicron (B.1.1.529) variants receptor binding domain (RBD) and antibody binding affinity, we return to investigate the new mutations seen in XBB.1.5 which is a descendant of Omicron. Using in silico ico modeling approaches against newer neutralizing antibodies that are shown effective against B.1.1.529, we predict the immune consequences of XBB.1.5s mutations and show that there is no statistically significant difference in overall antibody evasion when comparing to the B.1.1.529 and other related variants (e.g., BJ.1 and BM.1.1.1). However, noticeable changes in antibody binding affinity were seen due to specific amino acid changes of interest in the newer variants.

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Ford, C. T., Yasa, S., Jacob Machado, D. T., White, R. A., Janies, D. A.. 2023-02-13. Positing changes in neutralizing antibody activity for SARS-CoV-2 XBB.1.5 using in silico protein modeling. https://doi.org/10.1101/2023.02.10.528025

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