Rapid Development of Neutralizing and Diagnostic SARS-COV-2 Mouse Monoclonal Antibodies
Asheley Poole Chapman; Xiaoling Tang; Joo R. Lee; Asiya Chida; Kristina Mercer; Rebekah E. Wharton; Markus H Kainulainen; Jennifer L. Harcourt; Roosecelis B. Martines; Michelle Schroeder; Liangjun Zhao; Anton Bryksin; Bin Zhou; Eric Bergeron; Brigid C. Bollweg; Azaibi Tamin; Natalie Thornburg; David E. Wentworth; David Petway; Dennis Bagarozzi Jr.; M.G. Finn; Jason M. Goldstein.
Preprint
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| PREPRINT-BIORXIV | ID: ppbiorxiv-338095
The need for high-affinity, SARS-CoV-2-specific monoclonal antibodies (mAbs) is critical in the face of the global COVID-19 pandemic, as such reagents can have important diagnostic, research, and therapeutic applications. Of greatest interest is the ~300 amino acid receptor binding domain (RBD) within the S1 subunit of the spike protein because of its key interaction with the human angiotensin converting enzyme 2 (hACE2) receptor present on many cell types, especially lung epithelial cells. We report here the development and functional characterization of 29 nanomolar-affinity mouse SARS-CoV-2 mAbs created by an accelerated immunization and hybridoma screening process. Differing functions, including binding of diverse protein epitopes, viral neutralization, impact on RBD-hACE2 binding, and immunohistochemical staining of infected lung tissue, were correlated with variable gene usage and sequence.
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