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Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4 and BA.5

Wang, Qian, Guo, Yicheng, Iketani, Sho, Nair, Manoj S., Li, Zhiteng, Mohri, Hiroshi, Wang, Maple, Yu, Jian, Bowen, Anthony D., Chang, Jennifer Y., Shah, Jayesh G., Nguyen, Nadia, Chen, Zhiwei, Meyers, Kathrine, Yin, Michael T., Sobieszczyk, Magdalena E., Sheng, Zizhang, Huang, Yaoxing, Liu, Lihong, Ho, David D.·2022·Nature
DOI 10.1038/s41586-022-05053-wPMC PMC9385487

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Abstract

SARS-CoV-2 Omicron subvariants BA.2.12.1 and BA.4/5 have surged notably to become dominant in the United States and South Africa, respectively 1,2 . These new subvariants carrying further mutations in their spike proteins raise concerns that they may further evade neutralizing antibodies, thereby further compromising the efficacy of COVID-19 vaccines and therapeutic monoclonals. We now report findings from a systematic antigenic analysis of these surging Omicron subvariants. BA.2.12.1 is only modestly (1.8-fold) more resistant to sera from vaccinated and boosted individuals than BA.2. However, BA.4/5 is substantially (4.2-fold) more resistant and thus more likely to lead to vaccine breakthrough infections. Mutation at spike residue L452 found in both BA.2.12.1 and BA.4/5 facilitates escape from some antibodies directed to the so-called class 2 and 3 regions of the receptor-binding domain 3 . The F486V mutation found in BA.4/5 facilitates escape from certain class 1 and 2 antibodies but compromises the spike affinity for the viral receptor. The R493Q reversion mutation, however, restores receptor affinity and consequently the fitness of BA.4/5. Among therapeutic antibodies authorized for clinical use, only bebtelovimab retains full potency against both BA.2.12.1 and BA.4/5. The Omicron lineage of SARS-CoV-2 continues to evolve, successively yielding subvariants that are not only more transmissible but also more evasive to antibodies.

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  • The dominant new viral strain is the Omicron BA.5 which is the most antibody immune evasive against currently available vaccines.

    “The dominant new viral strain is the Omicron BA.5 which is the most antibody immune evasive against currently available vaccines9.”

    From The roles of APOBEC-mediated RNA editing in SARS-CoV-2 mutations, replication and fitness (2022) · cites this paper as [9]

  • Sequencing data of SARS-CoV-2 from patients revealed persistent accumulation of new mutations over the last two years of the Covid19 pandemic, leading to the emergence of new viral strains that can be more transmissible or virulent or evade vaccines.

    “However, sequencing data of SARS-CoV-2 from patients revealed persistent accumulation of new mutations over the last two years of the Covid19 pandemic, leading to the emergence of new viral strains that can be more transmissible or virulent5,6 or evade vaccines7–9.”

    From The roles of APOBEC-mediated RNA editing in SARS-CoV-2 mutations, replication and fitness (2022) · cites this paper as [9]

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Citations

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Research works printed but not linked: 27

  1. Khan, K. et al. Omicron sub-lineages BA.4/BA.5 escape BA.1 infection elicited neutralizing immunity. Preprint at medRxiv https://doi.org/10.1101/2022.04.29.22274477 (2022). · DOI
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  3. Zost, S. J. et al. Potently neutralizing and protective human antibodies against SARS-CoV-2. Nature 584, 443–449 (2020). · DOI · Paper page
  4. Jones, B. E. et al. The neutralizing antibody, LY-CoV555, protects against SARS-CoV-2 infection in nonhuman primates. Sci. Transl. Med. 13, eabf1906 (2021). · DOI
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  7. Westendorf, K. et al. LY-CoV1404 (bebtelovimab) potently neutralizes SARS-CoV-2 variants. Cell Rep. 39, 110812 (2022). · DOI
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  9. Li, D. et al. In vitro and in vivo functions of SARS-CoV-2 infection-enhancing and neutralizing antibodies. Cell 184, 4203–4219 e4232 (2021). · DOI
  10. Tortorici, M. A. et al. Broad sarbecovirus neutralization by a human monoclonal antibody. Nature 597, 103–108 (2021). · DOI
  11. Sheward, D. J. et al. Structural basis of Omicron neutralization by affinity-matured public antibodies. Preprint at bioRxiv https://doi.org/10.1101/2022.01.03.474825 (2022). · DOI
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  17. Geng, Q. et al. Structural basis for human receptor recognition by SARS-CoV-2 Omicron variant BA.1. J. Virol. 96, e0024922 (2022). · DOI
  18. Iketani, S. et al. Antibody evasion properties of SARS-CoV-2 Omicron sublineages. Nature 604, 553–556 (2022). · DOI
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  20. Tuekprakhon, A. et al. Antibody escape of SARS-CoV-2 Omicron BA.4 and BA.5 from vaccine and BA.1 serum. Cell https://doi.org/10.1016/j.cell.2022.06.005 (2022). · DOI
  21. Rössler, A. et al. BA.2 Omicron differs immunologically from both BA.1 Omicron and pre-Omicron variants. Preprint at medRxiv https://doi.org/10.1101/2022.05.10.22274906 (2022). · DOI
  22. Cao, Y. et al. BA.2.12.1, BA.4 and BA.5 escape antibodies elicited by Omicron infection. Nature https://doi.org/10.1038/s41586-022-04980-y (2022). · DOI
  23. Munoz-Fontela, C. et al. Animal models for COVID-19. Nature 586, 509–515 (2020). · DOI · Paper page
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Metadata

Authors
Wang, Q., Guo, Y., Iketani, S., Nair, M. S., Li, Z., Mohri, H., Wang, M., Yu, J., Bowen, A. D., Chang, J. Y., Shah, J. G., Nguyen, N., Chen, Z., Meyers, K., Yin, M. T., Sobieszczyk, M. E., Sheng, Z., Huang, Y., Liu, L., & Ho, D. D.
ORCID
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2022-07-05
Volume
608
Issue
7923
Pages
603-608
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/s41586-022-05053-w
PMC
PMC9385487
Cited by
775
References
9
Language
en
Licence

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