Author:
Chapman Asheley P.,Tang Xiaoling,Lee Joo R.,Chida Asiya,Mercer Kristina,Wharton Rebekah E.,Kainulainen Markus,Harcourt Jennifer L.,Martines Roosecelis B.,Schroeder Michelle,Zhao Liangjun,Bryksin Anton,Zhou Bin,Bergeron Eric,Bollweg Brigid C.,Tamin Azaibi,Thornburg Natalie,Wentworth David E.,Petway David,Bagarozzi Dennis A.,Finn M. G.,Goldstein Jason M.
Abstract
AbstractThe 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 nM-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.
Funder
Centers for Disease Control and Prevention
Georgia Institute of Technology
Publisher
Springer Science and Business Media LLC
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