C-terminal end of SAG2A protein interacts with innate immune response. (A) Three-dimensional model of recombinant SAG2A (rSAG2A) and the truncated form of the protein (rSAG2A∆135). Structural analysis shows that depletion of the C-terminal end did not affect the overall predicted three-dimensional structure or distribution of positive and negative charges along the protein. (B) Bone marrow-derived macrophages (BMMs) and (C) dendritic cells (BMDCs) were treated with different concentrations of rSAG2A and rSAG2A∆135 for 48 and 24 h, prior to determination of nitrite (B) and IL-12p40 levels (C), respectively. As controls, cells were left untreated (RPMI) or exposed to LPS (1 μg/ml) in similar time spam. Results are presented as mean ±SEM. Dashed lines indicate mean values obtained for untreated BMMs. * Statistical significance (p < 0.05) in relation to untreated controls.