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. 2020 Aug 28;11:1986. doi: 10.3389/fimmu.2020.01986

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Copyright © 2020 Alfaleh, Alsaab, Mahmoud, Alkayyal, Jones, Mahler and Hashem.

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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Schematic representation of different antibody formats. (A) Single chain fragment variable (scFv) composed of variable regions of the light chain (V_L) linked to variable regions of the heavy chain (V_H) by a flexible glycine-serine linker (Gly₄Ser)₃. (B) Nanobody fragments. (C) Fragment of antigen binding (Fab) composed of V_L and a constant domain of the light chain (CL) linked to V_H and constant domain 1 of the heavy chain (CH1) by a disulphide bond between the CL and CH1 domains. (D) Diabody composed of V_L linked to variable heavy V_H by a pentameric (Gly₄Ser). (E) F(ab)2 fragment composed of 2 × Fab fragments joined by an Immunoglobulin G (IgG) hinge region. (F) scFv fusion with an Fc IgG. (G) IgG composed of constant fragment (Fc), which is able to bind and stimulate immune effector cells, and Fab, which comprises the variable domains that contain the antigen binding regions. (H) Bispecific IgG antibody.