Liu, Chang, Zhou, Daming, Dijokaite-Guraliuc, Aiste, Supasa, Piyada, Duyvesteyn, Helen M E, Ginn, Helen M, Selvaraj, Muneeswaran, Mentzer, Alexander J, Das, Raksha, de Silva, Thushan I, and others. (2024) A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity. Cell Reports Medicine, . Article Number 101553. ISSN 2666-3791. (doi:10.1016/j.xcrm.2024.101553) (KAR id:105912)
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Official URL: https://doi.org/10.1016/j.xcrm.2024.101553 |
Abstract
BA.2.86, a recently described sublineage of SARS-CoV-2 Omicron, contains many mutations in the spike gene. It appears to have originated from BA.2 and is distinct from the XBB variants responsible for many infections in 2023. The global spread and plethora of mutations in BA.2.86 has caused concern that it may possess greater immune-evasive potential, leading to a new wave of infection. Here, we examine the ability of BA.2.86 to evade the antibody response to infection using a panel of vaccinated or naturally infected sera and find that it shows marginally less immune evasion than XBB.1.5. We locate BA.2.86 in the antigenic landscape of recent variants and look at its ability to escape panels of potent monoclonal antibodies generated against contemporary SARS-CoV-2 infections. We demonstrate, and provide a structural explanation for, increased affinity of BA.2.86 to ACE2, which may increase transmissibility.
Item Type: | Article |
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DOI/Identification number: | 10.1016/j.xcrm.2024.101553 |
Subjects: | Q Science > QR Microbiology > QR355 Virology |
Divisions: | Divisions > Division of Natural Sciences > Medway School of Pharmacy |
Funders: | Wellcome Trust (https://ror.org/029chgv08) |
Depositing User: | Nigel Temperton |
Date Deposited: | 10 May 2024 09:35 UTC |
Last Modified: | 13 May 2024 09:56 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/105912 (The current URI for this page, for reference purposes) |
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