| Issue |
Parasite
Volume 31, 2024
|
|
|---|---|---|
| Article Number | 39 | |
| Number of page(s) | 12 | |
| DOI | https://doi.org/10.1051/parasite/2024036 | |
| Published online | 09 July 2024 | |
Supplementary materials
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Supplementary Figure 1: Polyacrylamide gel electrophoresis stained with Coomassie brilliant blue of bacterial cells transformed with pBAD/TOPO® ThiofusionTM Expression System (ThermoFisher™) which expresses part of the EcCLP1 as a protein fused to thioredoxin (Thio-EcCLP1-his). Lane 1. Non-induced E. coli bacterial cells at 37 °C. Lane 2. Bacterial cells induced with 0.2% of arabinose at 37 °C. Positions of the molecular marker proteins with the corresponding masses in kilodaltons (kDa) are indicated. The arrow shows the recombinant-induced protein. |
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Supplementary Figure 2: Western-blot of recombinant Thio-EcCLP1-his protein stained with rabbit hyperimmune serum against Thio-EcCLP1-his. Lane 1. Preimmune rabbit serum, diluted 1/50 in PBS-milk 1.5%. Lane 2. Hyperimmune rabbit serum diluted 1/20. Lane 3. Same hyperimmune serum as in lane 2 but diluted 1/50. Lane 4. Same hyperimmune serum as in lane 2 but diluted 1/100. |
Supplementary Material 1: Sequence obtained from the mitochondrial cytochrome c oxidase subunit 1 (CO1) sequencing and primers employed for species and genotype determination of the protoscoleces utilized in this study. The genotype obtained correspond to G7 or pig strain. Access here
Supplementary Movie 1: Superposition of the ribbon representation of the crystal structure of human cathepsin (brown, [35]) and the modeled EcCLP1 (green). Magnified view at the active site. Access here
© A. Naidich et al., published by EDP Sciences, 2024
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