Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/171764
Title: Potent pan huACE2-dependent sarbecovirus neutralizing monoclonal antibodies isolated from a BNT162b2-vaccinated SARS survivor
Authors: Chia, Wan Ni
Tan, Chee Wah
Tan, Aaron Wai Kit
Young, Barnaby
Starr, Tyler N.
Lopez, Ester
Fibriansah, Guntur
Barr, Jennifer
Cheng, Samuel
Yeoh, Aileen Ying-Yan
Yap, Wee Chee
Lim, Beng Lee
Ng, Thiam-Seng
Sia, Wan Rong
Zhu, Feng
Chen, Shiwei
Zhang, Jinyan
Kwek, Madeline Sheng Si
Greaney, Allison J.
Chen, Mark
Au, Gough G.
Paradkar, Prasad N.
Peiris, Malik
Chung, Amy W.
Bloom, Jesse D.
Lye, David
Lok, Sheemei
Wang, Lin-Fa
Keywords: Science::Medicine
Issue Date: 2023
Source: Chia, W. N., Tan, C. W., Tan, A. W. K., Young, B., Starr, T. N., Lopez, E., Fibriansah, G., Barr, J., Cheng, S., Yeoh, A. Y., Yap, W. C., Lim, B. L., Ng, T., Sia, W. R., Zhu, F., Chen, S., Zhang, J., Kwek, M. S. S., Greaney, A. J., ...Wang, L. (2023). Potent pan huACE2-dependent sarbecovirus neutralizing monoclonal antibodies isolated from a BNT162b2-vaccinated SARS survivor. Science Advances, 9(30), eade3470-. https://dx.doi.org/10.1126/sciadv.ade3470
Journal: Science Advances 
Abstract: The emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern such as Omicron hampered efforts in controlling the ongoing coronavirus disease 2019 pandemic due to their ability to escape neutralizing antibodies induced by vaccination or prior infection, highlighting the need to develop broad-spectrum vaccines and therapeutics. Most human monoclonal antibodies (mAbs) reported to date have not demonstrated true pan-sarbecovirus neutralizing breadth especially against animal sarbecoviruses. Here, we report the isolation and characterization of highly potent mAbs targeting the receptor binding domain (RBD) of huACE2-dependent sarbecovirus from a SARS-CoV survivor vaccinated with BNT162b2. Among the six mAbs identified, one (E7) showed better huACE2-dependent sarbecovirus neutralizing potency and breadth than any other mAbs reported to date. Mutagenesis and cryo-electron microscopy studies indicate that these mAbs have a unique RBD contact footprint and that E7 binds to a quaternary structure-dependent epitope.
URI: https://hdl.handle.net/10356/171764
ISSN: 2375-2548
DOI: 10.1126/sciadv.ade3470
Schools: Lee Kong Chian School of Medicine (LKCMedicine) 
Organisations: National Center of Infectious Diseases, Singapore 
Tan Tock Seng Hospital 
Rights: © 2023 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Journal Articles

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