Open Access
Research Article
Volume 29, 2022
Article Number 16
Number of page(s) 13
Published online 22 March 2022

Supplementary Material

thumbnail Supplementary Figure 1

Nucleotide and deduced amino acid sequences of GSTO2 gene of F. hepatica. The start and stop codons are indicated in bold and “*”. The conservative cysteine residues are shown by a box, while the GST_N and GST_C regions are indicated by underline and wave, respectively. The α-helicals, β-strands, glutaredoxin active site and glutathione-binding residues are marked in shadow, red and italic, respectively.

thumbnail Supplementary Figure 2

Comparisons of the amino acid sequence of GSTO2 protein of F. hepatica with other trematode GSTO. The red shadow indicates that the sequence consistency is 100%, while similar residues are shown as blue box. Fh: Fasciola hepatica (AFX98104.1); Fg: Fasciola gigantica (JX157881.1); Sm: Schistosoma mansoni (AAO49385.1); Cs: Clonorchis sinensis (KX163089.1).

thumbnail Supplementary Figure 3

Identification of rGSTO2 protein of F. hepatica by SDS-PAGE and western blot. (A) Lane M, protein marker; lane 1, Sonicated supernatant of cultures after transformation of E. coli with the empty pET-28a plasmid; lane 2, lysate precipitation of rGSTO2 after induction for 6 h; lane 3-6, lysate supernatant of rGSTO2 at 2, 4, 6 and 8 hours induced by IPTG. (B) Lane M, protein marker; lane 1, purified rGSTO2 protein. (C) Lane M, protein marker; lane 1 and lane 2 were loaded with rGSTO2 protein and then incubated with sheep anti-F. hepatica sera or normal sheep serum, then incubated with HRP-conjugated rabbit anti-sheep IgG. (D) Lane M, protein marker; lane 1 and lane 2 were loaded with rGSTO2 protein and then incubated with mouse anti-rGSTO2 IgG or naïve mouse serum, respectively, and then incubated with HRP-conjugated goat anti-mouse IgG.

© X. Wang et al., published by EDP Sciences, 2022

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