Fig. 2: Epitope specificity, agonist activity and sTREM2 binding of anti-TREM2 antibodies. | Nature Communications

Fig. 2: Epitope specificity, agonist activity and sTREM2 binding of anti-TREM2 antibodies.

From: Rapid affinity optimization of an anti-TREM2 clinical lead antibody by cross-lineage immune repertoire mining

Fig. 2

a Summary of binding of antibodies 3.10C2 and Para.09 to TREM2 peptides with Ala mutations in individual positions (Gly for position 153). Values are ratios of wild-type to Ala mutant peptide kd, highlighted as indicated by the scale. The two residues flanking the TREM2 cleavage site are shown in orange. Residues with side-chains in the binding interface of both hu3.10C2 and huPara.09 in the complex structures are indicated with asterisks, with the most structurally significant contacts highlighted in red. b Agonist activity of soluble IgG of 3.10A7 and 3.10C2 parallel lineage and clonal variants in Jurkat-NFAT-TREM2-DAP12 cell reporter cells. The dotted line indicates baseline activation by control mouse IgG2a. c Binding of anti-TREM2 antibodies to sTREM2 from bone marrow-derived macrophage (BMDM) cultures from transgenic mice expressing hTREM2, normalized to control antibody 16B8 binding. Bars and errors indicate average and standard deviation of 2 to 4 repeats in panel b. Luc RLU, luciferase relative luminosity units. Source data are provided as a Source Data file.

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