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. 2023 Aug 22;14:1222267. doi: 10.3389/fimmu.2023.1222267

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Copyright © 2023 Ferguson, Delgado, McBride, Orbe, La Vake, Caimano, Mendez, Moraes, Schryvers, Moody, Radolf, Weiner and Hawley

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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Heavy and light chains used to form full-length mAbs. (A) Five heavy and three light chains (HC and LC, respectively) were fused to a mouse IgG2 constant domain to form five distinct full-length mAbs. A multiple sequence alignment of the (B) HCs and (C) LCs. The amino acid residues with a consensus identity of over 51% are represented by gray shading, while lowercase letters indicate amino acids with a mismatched identity. HC and LC CDRs predicted using abYsis (34) are denoted by cyan or pink shading, respectively. Asterisk (*) indicates a non-conserved residue in all three LC CDR3s.