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Rapid escape of new SARS-CoV-2 Omicron variants from BA.2-directed antibody responses.
- Source :
- Cell Reports; Apr2023, Vol. 42 Issue 4, pN.PAG-N.PAG, 1p
- Publication Year :
- 2023
-
Abstract
- In November 2021, Omicron BA.1, containing a raft of new spike mutations, emerged and quickly spread globally. Intense selection pressure to escape the antibody response produced by vaccines or severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection then led to a rapid succession of Omicron sub-lineages with waves of BA.2 and then BA.4/5 infection. Recently, many variants have emerged such as BQ.1 and XBB, which carry up to 8 additional receptor-binding domain (RBD) amino acid substitutions compared with BA.2. We describe a panel of 25 potent monoclonal antibodies (mAbs) generated from vaccinees suffering BA.2 breakthrough infections. Epitope mapping shows potent mAb binding shifting to 3 clusters, 2 corresponding to early-pandemic binding hotspots. The RBD mutations in recent variants map close to these binding sites and knock out or severely knock down neutralization activity of all but 1 potent mAb. This recent mAb escape corresponds with large falls in neutralization titer of vaccine or BA.1, BA.2, or BA.4/5 immune serum. [Display omitted] • 25 potent RBD mAbs generated from vaccinees suffering BA.2 breakthrough infections • Potent mAbs bind 3 clusters, 2 correspond to early-pandemic binding hotspots • RBD mutations in recent variants map close to these binding sites • Neutralization activity of all but 1 potent mAb is reduced Dijokaite-Guraliuc et al. analyze potently neutralizing antibodies from vaccinated individuals with BA.2 breakthrough infections. The antibodies bind 3 sites on the receptor-binding domain, 2 of which are in common with early-pandemic antibodies. Mutations in more recent variants map closely to these sites, leading to reduced neutralization in all but one mAb. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 26391856
- Volume :
- 42
- Issue :
- 4
- Database :
- Complementary Index
- Journal :
- Cell Reports
- Publication Type :
- Academic Journal
- Accession number :
- 163292462
- Full Text :
- https://doi.org/10.1016/j.celrep.2023.112271