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. Author manuscript; available in PMC: 2023 May 23.
Published in final edited form as: Cell. 2022 Mar 17;185(6):995–1007.e18. doi: 10.1016/j.cell.2022.02.023

Figure 1. Initial characterization of neutralizing monoclonal antibodies (mAbs) cloned from Ebola virus (EBOV) and Sudan virus (SUDV) glycoprotein (GP) dual-binding memory B cells.

Figure 1.

(A) Neutralization of live EBOV, SUDV, or BDBV by the indicated monoclonal antibodies (mAbs) was assessed by plaque assay. Left: Neutralization of EBOV by varying concentrations of each mAb. Right: Summary table showing the 50 or 80% plaque reduction neutralization test (PRNT50 or PRNT80) for each mAb against the indicated viruses. (B) Grouping of the neutralizing mAbs into competition groups. The numbers in the table represent the binding of fluorescently labeled mAbs (columns) to EBOV GP-expressing cells in the presence of excess unlabeled competitor mAbs (rows). Binding in the presence of each competitor is expressed as a percentage of the fluorescence signal in the absence of competitor. mAbs were classified as soluble glycoprotein (sGP)-binding (+) or non-binding (−) by enzyme-linked immunosorbent assay (ELISA). mAb 9.20.1C3 was unique within the chalice bowl competition group in being unable to bind to sGP (yellow highlight).