Figure 2From: SAG2A protein from Toxoplasma gondii interacts with both innate and adaptive immune compartments of infected hostsAnchorage site, carbon structure and charge distribution of SAG2A protein. (A) SAG2A anchorage in Toxoplasma gondii’s surface surface by glycosyl-phosphatidylinositol (GPI) was predicted to be in a leucin at position 169 of its amino acid sequence, located at the C-terminal end of SAG2A. (B) The modeled carbon structure of SAG2A evidences a disordered amino acid sequence, absent in the SAG1 and BSR4 proteins. (C) The C-terminal end of SAG2A presents a relevant hydrophobic portion, with distinct polar amino acids at positions 134 and 137.Back to article page