bioRxivBiochemistry
Predicting changes in neutralizing antibody activity for SARS-CoV-2 XBB.1.5 using in silico protein modeling
C. T. Ford, S. Yasa, D. T. Jacob Machado, R. A. White, D. A. Janies
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.
- assay: protein structure
- research focus: drug response / drug discovery
- research focus: protein structure prediction
- approach: deep learning
- approach: statistical model
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Predictions of the SARS-CoV-2 Omicron Variant (B.1.1.529) Spike Protein Receptor-Binding Domain Structure and Neutralizing Antibody Interactions
Colby T. Ford, Denis Jacob Machado, Daniel A. Janies·Frontiers in VirologyPeer-reviewed·Feb 6, 2022
- Alarming antibody evasion properties of rising SARS-CoV-2 BQ and XBB subvariants
Q. Wang, S. Iketani, … D. D. Ho·bioRxiv·Nov 23, 2022
- Predicting Antibody and ACE2 Affinity for SARS-CoV-2 BA.2.86 and JN.1 with In Silico Protein Modeling and Docking
Shirish Yasa, Sayal Guirales-Medrano, … Daniel A. Janies·bioRxiv·Nov 22, 2023
- XBB.1.5 monovalent booster improves antibody binding and neutralization against emerging SARS-CoV-2 Omicron variants
S. Jain, S. Kumar, … M. S. Suthar·bioRxiv·Feb 3, 2024
- Assessment of neutralization susceptibility of Omicron subvariants XBB.1.5 and BQ.1.1 against broad-spectrum neutralizing antibodies through epitopes mapping
- Antibody Neutralization of Emerging SARS-CoV-2: EG.5.1 and XBC.1.6