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Article

Development and Characterization of Phage-Display-Derived Novel Human Monoclonal Antibodies against the Receptor Binding Domain of SARS-CoV-2

1
Department of Chemistry, Kookmin University, Seoul 02707, Republic of Korea
2
Research Center, SG Medical, Seoul 05548, Republic of Korea
3
Department of Biopharmaceutical Chemistry, Kookmin University, Seoul 02707, Republic of Korea
4
Department of Life Sciences, Ewha Womans University, Seoul 03760, Republic of Korea
5
Biopharmaceutical Chemistry Major, School of Applied Chemistry, Kookmin University, Seoul 02707, Republic of Korea
6
Antibody Research Institute, Kookmin University, Seoul 02707, Republic of Korea
*
Author to whom correspondence should be addressed.
Biomedicines 2022, 10(12), 3274; https://doi.org/10.3390/biomedicines10123274
Submission received: 22 November 2022 / Revised: 14 December 2022 / Accepted: 15 December 2022 / Published: 17 December 2022
(This article belongs to the Special Issue Biomedicines: 10th Anniversary)

Abstract

Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has resulted in an ongoing global pandemic crisis, caused by the life-threatening illness coronavirus disease 2019 (COVID-19). Thus, the rapid development of monoclonal antibodies (mAbs) to cope with COVID-19 is urgently necessary. In this study, we used phage display to develop four human mAbs specific to the receptor-binding domain (RBD) of SARS-CoV-2. Our intensive in vitro functional analyses demonstrated that K102.1, an anti-SARS-CoV-2 RBD-specific mAb, exerted potent neutralizing activity against pseudoviral and live viral infection and the interaction between SARS-CoV-2 RBD and human angiotensin-converting enzyme 2. Monotherapy with K102.1 also revealed the therapeutic potential against SARS-CoV-2 infection in vivo. Further, this study developed a sandwich enzyme-linked immunosorbent assay with a non-competing mAb pair, K102.1 and K102.2, that accurately detected the RBDs of SARS-CoV-2 wild-type and variants with high sensitivity in the picomolar range. These findings suggest that the phage-display-based mAb selection from an established antibody library may be an effective strategy for the rapid development of mAbs against the constantly evolving SARS-CoV-2.
Keywords: SARS-CoV-2; human antibody; neutralization; sandwich ELISA SARS-CoV-2; human antibody; neutralization; sandwich ELISA
Graphical Abstract

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MDPI and ACS Style

Kim, J.W.; Min, S.W.; Lee, J.; Shin, H.G.; Choi, H.L.; Yang, H.R.; Lee, J.H.; Cho, Y.B.; Shim, H.; Lee, S. Development and Characterization of Phage-Display-Derived Novel Human Monoclonal Antibodies against the Receptor Binding Domain of SARS-CoV-2. Biomedicines 2022, 10, 3274. https://doi.org/10.3390/biomedicines10123274

AMA Style

Kim JW, Min SW, Lee J, Shin HG, Choi HL, Yang HR, Lee JH, Cho YB, Shim H, Lee S. Development and Characterization of Phage-Display-Derived Novel Human Monoclonal Antibodies against the Receptor Binding Domain of SARS-CoV-2. Biomedicines. 2022; 10(12):3274. https://doi.org/10.3390/biomedicines10123274

Chicago/Turabian Style

Kim, Ji Woong, Sung Won Min, Jichul Lee, Ha Gyeong Shin, Hye Lim Choi, Ha Rim Yang, Ji Hyun Lee, Yea Bin Cho, Hyunbo Shim, and Sukmook Lee. 2022. "Development and Characterization of Phage-Display-Derived Novel Human Monoclonal Antibodies against the Receptor Binding Domain of SARS-CoV-2" Biomedicines 10, no. 12: 3274. https://doi.org/10.3390/biomedicines10123274

APA Style

Kim, J. W., Min, S. W., Lee, J., Shin, H. G., Choi, H. L., Yang, H. R., Lee, J. H., Cho, Y. B., Shim, H., & Lee, S. (2022). Development and Characterization of Phage-Display-Derived Novel Human Monoclonal Antibodies against the Receptor Binding Domain of SARS-CoV-2. Biomedicines, 10(12), 3274. https://doi.org/10.3390/biomedicines10123274

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