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. 2020 Jan 21;10:3086. doi: 10.3389/fimmu.2019.03086

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Copyright © 2020 Levin, Evans, Bort, Rickel, Lewis, Wu, Hoover, MacNeil, La, Wolfson, Rixon, Dillon, Kornacker, Swanson and Peng.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Directed evolution of ICOSL by yeast display leads to recombinant vIgD hits with enhanced binding to ICOS and CD28. ICOSL DNA sequences derived from yeast display outputs were cloned into a mammalian expression vector and produced in HEK-293 cells. Engineered ICOSL vIgD-Fc were subsequently titrated on CD28 (left) and ICOS (right) transfectants. Binding was detected by flow cytometry and Mean Fluorescence Intensity (MFI) was plotted vs. protein concentration. For comparison, ICOSL vIgD-Fc derived from 1st generation (A160), 2nd generation (A2237), and 3rd generation (A3256) are compared to WT ICOSL, showing progressive increases in binding for each target.