Abigail G. Esposito
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Abigail G. Esposito has a total of 14 co-authors. Here are the top co-authors by number of shared publications:
- Charles R. Crain
Ragon Institute of MGB, MIT and Harvard, Cambridge, MA, USA
1 shared publication - Edward D. Lamperti
The Ragon Institute of Mass General, MIT, and Harvard 1 , Cambridge, MA
1 shared publication - Facundo D. Batista
The Ragon Institute of Mass General, MIT, and Harvard 1 , Cambridge, MA
1 shared publication - Gaurav D. Gaiha
Ragon Institute of Mass General, MIT and Harvard, Cambridge, USA
1 shared publication - Gordon A. Dale
The Ragon Institute of Mass General Brigham, MIT, and Harvard 1 Batista Lab Cambridge, MA
1 shared publication - Ian A. Wilson
Department of Integrative Structural and Computational Biology, The Scripps Research Institute
1 shared publication
Latest Publications
- 17 July 2025
- Published by Rockefeller University Press in Journal of Experimental Medicine
- Vol. 222 (10)
In vivo antibody diversification targeting a conserved coronavirus epitope
To explore the use of human B cell receptor (BCR) knock-in mice for broadening antibody responses, we diversified CR3022, a monoclonal antibody (mAb) originally identified in a 2003 severe acute respiratory syndrome coronavirus (SARS-CoV) convalescent patient. This mAb targets a conserved epitope on the coronavirus receptor-binding domain (RBD). We took advantage of high- and low-affinity CR3022 BCR knock-in mice and immunized them with SARS-CoV-2 Wuhan RBD trimers to expand the breadth of these antibodies toward this virus. The resulting antibodies retained the ability to neutralize SARS-CoV and exhibited enhanced affinity and neutralization against the SARS-CoV-2 WA1/2020 strain, as well as the Delta (B.1.617.2) and Omicron KP.3 variants. They also showed broadened reactivity to two bat coronaviruses: WIV1 and, to a lesser potency, BtKY72. Structural analysis revealed key mutations that enhanced binding and neutralization, highlighting the importance of epitope accessibility and variant-specific conformations in antibody diversification. These findings demonstrate that human BCR-expressing mouse models can generate effective antibodies with broad neutralizing activity against viral epitopes.
- 17 July 2025
- Published by Rockefeller University Press in Journal of Experimental Medicine
- Vol. 222 (10)
In vivo antibody diversification targeting a conserved coronavirus epitope
To explore the use of human B cell receptor (BCR) knock-in mice for broadening antibody responses, we diversified CR3022, a monoclonal antibody (mAb) originally identified in a 2003 severe acute respiratory syndrome coronavirus (SARS-CoV) convalescent patient. This mAb targets a conserved epitope on the coronavirus receptor-binding domain (RBD). We took advantage of high- and low-affinity CR3022 BCR knock-in mice and immunized them with SARS-CoV-2 Wuhan RBD trimers to expand the breadth of these antibodies toward this virus. The resulting antibodies retained the ability to neutralize SARS-CoV and exhibited enhanced affinity and neutralization against the SARS-CoV-2 WA1/2020 strain, as well as the Delta (B.1.617.2) and Omicron KP.3 variants. They also showed broadened reactivity to two bat coronaviruses: WIV1 and, to a lesser potency, BtKY72. Structural analysis revealed key mutations that enhanced binding and neutralization, highlighting the importance of epitope accessibility and variant-specific conformations in antibody diversification. These findings demonstrate that human BCR-expressing mouse models can generate effective antibodies with broad neutralizing activity against viral epitopes.