A group of chimeric antigen receptors (CARS)
A technology of chimeric antigen receptors and antigens, applied in the direction of antibodies, antibody medical components, antibody mimics/scaffolds, etc., can solve problems such as the destruction of healthy tissues
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Embodiment 1
[0388] Example 1: Generation of rcSso7d-based low-affinity single-domain binding moieties for CAR panels according to the invention
[0389] In a first example it is shown a strategy for generating an antigen-binding moiety with low affinity suitable for use as an antigen-binding moiety of a CAR panel according to the invention. Reduced charge Sso7d (rcSso7d) is a reduced charge version of a small (-7 kDa) DNA-binding protein from the archaea Sulfolobus solfataricus. The reduced charge minimizes non-specific binding, due to reduced electrostatic interactions. rcSso7d is a single-domain protein antigen-binding moiety with high thermal stability and monomeric behavior, and is thus an example suitable for binding to scaffolds. Starting with the well-characterized antigen-binding portion rcSso7d E11.4.1, which binds to human EGFR with a K of 19 nM d Combined with (Traxlmayr et al., JBiol Chem. 2016; 291(43):22496-22508), by performing an alanine scan in which we replaced all ami...
Embodiment 2
[0404] Example 2: Extracellular disulfide bonds formed by cysteines prevent avidity effects that fully utilize the AND gate function of the CAR group
[0405] Extracellular disulfide bonds formed by cysteines in the extracellular hinge region, eg CD8α, prevent the use of the avidity effect according to the invention. This is demonstrated in Example 2, where a low-affinity mutant of the binding moiety "E11.4.1G32A" of Example 1 is fused to the CAR signaling backbone with two extracellular cysteine residues in the hinge region of CD8α (UniProt ID P01732, positions C164 and C181) were substituted or not substituted with serine residues, respectively. While cysteine-containing CAR variants ("Cys") efficiently triggered T cell activation in response to target cells, serine-containing variants ("Ser") did not or only weakly triggered T cells. Thus, this example illustrates the importance of preventing disulfide bond formation when generating CAR molecules suitable for use in CAR ...
Embodiment 3
[0419] Example 3: Single-chain variable fragments (scFv) can trigger clustering of CARs in cell membranes, thereby preventing avidity effects using combinations of specific recognition antigens
[0420] The third example shows that the integration of scFv-based binding moieties in CAR molecules can prevent avidity effects utilizing combinations of specific recognition antigens. Figure 4 Schematic representation of the CAR construct shown in A showing the CAR variants tested (4D5-5-8cys-BB-3z, 4D5-5-8ser-BB-3z, 4D5-5(split)-8ser-BB-FKBP (36V )-3z) design. In the example shown, scFv 4D5-5 directed against HER2 was used as the antigen binding moiety and incorporated into a monomeric ("Ser") or dimeric ("Cys") CAR signaling backbone. Figure 4 B shows CAR expression in primary T cells. The effective binding affinity of scFv 4D5-5 was reported as 1.1 μΜ (Liu et al., Cancer Res. 2015; 75(17):3596-3607), which is comparable to the affinity of E11.4.1-G32A. Jurkat T cells expressi...
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