Nature Communications (Jan 2023)
Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2
- Kuan-Ying A. Huang,
- Xiaorui Chen,
- Arpita Mohapatra,
- Hong Thuy Vy Nguyen,
- Lisa Schimanski,
- Tiong Kit Tan,
- Pramila Rijal,
- Susan K. Vester,
- Rory A. Hills,
- Mark Howarth,
- Jennifer R. Keeffe,
- Alexander A. Cohen,
- Leesa M. Kakutani,
- Yi-Min Wu,
- Md Shahed-Al-Mahmud,
- Yu-Chi Chou,
- Pamela J. Bjorkman,
- Alain R. Townsend,
- Che Ma
Affiliations
- Kuan-Ying A. Huang
- Graduate Institute of Immunology and Department of Pediatrics, National Taiwan University Hospital, College of Medicine, National Taiwan University
- Xiaorui Chen
- Genomics Research Center, Academia Sinica
- Arpita Mohapatra
- Genomics Research Center, Academia Sinica
- Hong Thuy Vy Nguyen
- Genomics Research Center, Academia Sinica
- Lisa Schimanski
- MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital
- Tiong Kit Tan
- MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital
- Pramila Rijal
- MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital
- Susan K. Vester
- Department of Biochemistry, University of Oxford
- Rory A. Hills
- Department of Biochemistry, University of Oxford
- Mark Howarth
- Department of Biochemistry, University of Oxford
- Jennifer R. Keeffe
- Division of Biology and Biological Engineering, California Institute of Technology
- Alexander A. Cohen
- Division of Biology and Biological Engineering, California Institute of Technology
- Leesa M. Kakutani
- Division of Biology and Biological Engineering, California Institute of Technology
- Yi-Min Wu
- Institute of Biological Chemistry, Academia Sinica
- Md Shahed-Al-Mahmud
- Genomics Research Center, Academia Sinica
- Yu-Chi Chou
- Biomedical Translation Research Center, Academia Sinica
- Pamela J. Bjorkman
- Division of Biology and Biological Engineering, California Institute of Technology
- Alain R. Townsend
- MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital
- Che Ma
- Genomics Research Center, Academia Sinica
- DOI
- https://doi.org/10.1038/s41467-023-35949-8
- Journal volume & issue
-
Vol. 14,
no. 1
pp. 1 – 13
Abstract
An antibody, IY-2A, identified from a panel of class-4 SARS-CoV-2-neutralizing antibodies isolated from convalescent and vaccinated individuals, targets and induces partial unfolding of a conserved epitope within the RBD. IY-2A retains activity against BA.4/5 subvariants and neutralizes diverse sarbecoviruses.
