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Fig. 6 | BMC Structural Biology

Fig. 6

From: Leishmania infantum 5’-Methylthioadenosine Phosphorylase presents relevant structural divergence to constitute a potential drug target

Fig. 6

Characterization of the polyclonal antibody directed against an antigenic C-terminal peptide of LiMTAP. a C-terminal location of the surface antigenic peptide unique to LiMTAP. The peptide includes amino acids 277 to 300, colored in yellow or brown. Residues identified as highly exposed through I-TASSER (E283, H284, A287, E288, Q291, S299) are colored in brown. b Specificity of the C-terminal Li-peptide was tested by western blot using respectively the LiMTAP antibody, and the β-actin antibody as a control for human PBMC lysates. The total proteins extracted from Leishmania and human PBMC were resolved on 12% SDS-PAGE gel, transferred to PVDF membrane and then subjected to western blot analysis using anti-LiMTAP (1/10000) or anti-β-actin (1/5000) antibodies. The Figure is representative of three independent experiments. Lanes: (1) Prestained marker MW in kDa (Vivantis, CA, USA); (2) Human PBMC lysates; (3), (4) and (5): 3, 7 and 15 micrograms of L. infantum (LV50) promastigote lysates, respectively

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