A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity
Issued Date
2024-05-21
Resource Type
eISSN
26663791
Scopus ID
2-s2.0-85193448044
Pubmed ID
38723626
Journal Title
Cell Reports Medicine
Volume
5
Issue
5
Rights Holder(s)
SCOPUS
Bibliographic Citation
Cell Reports Medicine Vol.5 No.5 (2024)
Suggested Citation
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. A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity. Cell Reports Medicine Vol.5 No.5 (2024). doi:10.1016/j.xcrm.2024.101553 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/98457
Title
A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity
Author(s)
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.
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.
Author's Affiliation
Mahidol Oxford Tropical Medicine Research Unit
NIHR Oxford Biomedical Research Centre
Medway School of Pharmacy
Diamond Light Source
University of Oxford
Sheffield Teaching Hospitals NHS Foundation Trust
Sir William Dunn School of Pathology
Nuffield Department of Medicine
University of Oxford Medical Sciences Division
The University of Sheffield
Centre for Free-Electron Laser Science
NIHR Oxford Biomedical Research Centre
Medway School of Pharmacy
Diamond Light Source
University of Oxford
Sheffield Teaching Hospitals NHS Foundation Trust
Sir William Dunn School of Pathology
Nuffield Department of Medicine
University of Oxford Medical Sciences Division
The University of Sheffield
Centre for Free-Electron Laser Science
Corresponding Author(s)
Other Contributor(s)
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.