Figure 1 | Scientific Reports

Figure 1

From: Implementing a method for engineering multivalency to substantially enhance binding of clinical trial anti-SARS-CoV-2 antibodies to wildtype spike and variants of concern proteins

Figure 1

Reformatting anti-SARS-CoV-2 antibodies into tetrameric proteins. The clinical stage antibodies REGN10987, REGN10933 and CB6/Junshi are IgG1 immunoglobulins and were redesigned into various tetrameric Quad proteins. IgG1 is depicted in (A) showing heavy and light chain variable (V) regions, the light chain constant (C) region that is disulphide bonded to the heavy chain CH1 domain, the two heavy chains are disulphide bonded between the hinge regions. Four tetramer formats were developed. (B); scFv-TD comprising VH and VL joined by a flexible linker and fused to the p53 tetramerization domain (TD). This complex is a tetravalent scFv. (C): Fab-TD comprising the Fab fragment of IgG with the TD fused to the heavy chain CH1. This complex is tetravalent for the Fab. (D) Ig-TD comprising a heavy and a light chain with the TD fused to the heavy chain CH3. This forms a complex with the TDs and disulphide bonding between the heavy chain hinge regions. (E) mIg-TD is like Ig-TD but lacks the hinge region. This forms a complex with the TDs without disulphide bonding between the heavy chain hinge regions.

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