A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity.
Liu, C., Zhou, D., Dijokaite-Guraliuc, A., Supasa, P., Duyvesteyn, H.M.E., Ginn, H.M., Selvaraj, M., Mentzer, A.J., Das, R., de Silva, T.I., Ritter, T.G., Plowright, M., Newman, T.A.H., Stafford, L., Kronsteiner, B., Temperton, N., Lui, Y., Fellermeyer, M., Goulder, P., Klenerman, P., Dunachie, S.J., Barton, M.I., Kutuzov, M.A., Dushek, O., Fry, E.E., Mongkolsapaya, J., Ren, J., Stuart, D.I., Screaton, G.R.(2024) Cell Rep Med 5: 101553-101553
- PubMed: 38723626
- DOI: https://doi.org/10.1016/j.xcrm.2024.101553
- Primary Citation of Related Structures:
8QRF, 8QRG, 8QSQ, 8QTD, 8R80, 8R8K - PubMed 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.
Organizational Affiliation:
Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK; Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.