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Original Article

Molecular Cloning and Characterization of a P38-Like Mitogen-Activated Protein Kinase from Echinococcus granulosus

Guodong Lü1, Jing Li1,2, Chuanshan Zhang1, Liang Li1, Xiaojuan Bi1, Chaowang Li1, Jinliang Fan1, Xiaomei Lu1, Dominique A. Vuitton3, Hao Wen1,*, Renyong Lin1,*
The Korean Journal of Parasitology 2016;54(6):759-768.
Published online: December 31, 2016

1Xinjiang Key Laboratory of Echinococcosis, Clinical Medical Research Institute, The First Affiliated Hospital of Xinjiang Medical University, Urumqi, Xinjiang, 830054, P. R. 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*Corresponding authors (renyong_lin@sina.com; dr.wenhao@163.com)
• Received: March 29, 2016   • Revised: September 29, 2016   • Accepted: October 4, 2016

Copyright © 2016 by The Korean Society for Parasitology and Tropical Medicine

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Molecular Cloning and Characterization of a P38-Like Mitogen-Activated Protein Kinase from Echinococcus granulosus
Korean J Parasitol. 2016;54(6):759-769.   Published online December 31, 2016
DOI: https://doi.org/10.3347/kjp.2016.54.6.759
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Molecular Cloning and Characterization of a P38-Like Mitogen-Activated Protein Kinase from Echinococcus granulosus
Korean J Parasitol. 2016;54(6):759-769.   Published online December 31, 2016
DOI: https://doi.org/10.3347/kjp.2016.54.6.759
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Molecular Cloning and Characterization of a P38-Like Mitogen-Activated Protein Kinase from Echinococcus granulosus
Image Image Image Image Image Image Image Image
Fig. 1 Alignment of the deduced Egp38 amino acid sequence with other relevant sequences. Amino acid residues that are conserved in at least 2 proteins are indicated in white on a black background. Homologies of the aligned proteins to Egp38 are indicated at the end of the alignment (% identity). Asterisks denote residues that are highly conserved in eukaryotic protein kinases [37]. Black triangles indicate conserved Asp residues within the docking domain [38]. Thr and Tyr residues of the conserved T-G-Y motif are denoted by ‘P’. Black rectangles indicate residues in the yeast HOG1 that, when mutated, lead to constitutive activation [39]. Circles above the alignment indicate residues in the human p38 MAPK-α that are involved in the binding of pyridinyl imidazole inhibitors [39]. The activation loop is marked by a dotted line below the aligned sequence. Egp38 (ACT21201.1), E. multilocularis p38 MAPK (EmMPK2; CAQ34816.1), H. sapiens p38 MAPK-α (Hsp38α; Q16539), D. melanogaster p38 MAPK (DmMK14A; O62618), C. elegans stress-activated protein kinase PMK-1 (CePMK1; Q17446), and S. cerevisiae HOG-1 (ScHOG1; P32485).
Fig. 2 Phylogenetic tree of p38 in E. granulosus and other relevant species. E. granulosus p38 MAPK (egp38.pro; ACT21201.1), E. multilocularis p38 MAPK (emmpk2.pro; CAQ34816.1), H. sapiens p38 MAPK-α (hsp38-alpha.pro; Q16539), H. sapiens p38 MAPK-β (hsp38-beta.pro; Q15759), H. sapiens p38 MAPK-γ (hsp38-gama.pro; P53778), H. sapiens p38 MAPK-δ (hsp38-delta.pro; O15264), C. elegans stress-activated protein kinase PMK-1 (cepmk1.pro; Q17446), Danio rerio Mapk14b protein (drmapk14.pro; AAH63937.1), Xenopus tropicalis MAPK 11 (xtmpk11.pro; NP_001098754.1), S. japonicum MAPK14a (sjmpk14; CAX72870), Brugia malayi p38 map kinase family protein 2 isoform b (bmp38.pro; A8PQS0), Loa loa CMGC/MAPK/p38 protein kinase (llp38.pro; XP_003141640), Wuchereria bancrofti CMGC/MAPK/P38 protein kinase (wbp38.pro; WUBG14523.1 of Broad Institute Filarial Database), D. melanogaster p38 MAPK (dmmk14.pro; O62618), and yeast HOG-1 (schog1.pro; P32485).
Fig. 3 Molecular models of the tertiary structure. (A) Surface rendering of Egp38. (B) Surface rendering of EmMPK2. (C) Surface rendering of Hsp38α. Individual sub-domains (helix and strand) are colored in the following order: gray, deep blue, sky blue, green, kelly green, yellow, khaki, orange, and red.
Fig. 4 Egp38 mRNA levels in larval stages.
Fig. 5 Egp38 antibody reactivities. (A) Total proteins were separated by SDS-PAGE. (B) The Egp38 protein was identified with an anti-p38 antibody. (C) The Egp38 protein was identified with an anti-phospho-p38 (pTGpY) antibody. (D) β-actin protein of E. granulosus was identified with an anti-β-actin antibody. Lane 1, E. granulosus protoscolices lysates; lane 2, E. granulosus vesicle lysates. Arrows indicate the interest proteins.
Fig. 6 Immunohistochemical detection of Egp38 in E. granulosus larval stages. Paraffin sections of protoscolices and vesicles isolated from CE sheep were probed with rabbit anti-Egp38 (A, D) and anti-phospho-p38 primary antibodies (B, E) and developed with a peroxidase-coupled goat anti-rabbit IgG secondary antibody or with secondary antibody alone (C, F). The following structures are indicated: GL, germinal layer; LL, laminated layer; P, protoscolex; R, rostellum; S, sucker. Arrows indicate the locations of Egp38 or the active form of Egp38. Scale bar=50 μm.
Fig. 7 Effects of the p38 MAPK inhibitor ML3403 on the viability of cultivated protoscolices in vitro. (A) Survival rates of protoscolices after 5 days of treatment with different concentrations of ML3403. (B) Egp38 activity in inhibitor-treated protoscolices. Protoscolices were incubated with the inhibitor ML3403 (60 μM) for 4 hr (lane 4). Lysates were examined by western blotting using antibodies against phosphorylated p38 MAPK (P-Egp38) as well as non-phosphorylated (Egp38). Lane 1, protoscolices prior to treatment. Lane 2, untreated protoscolices grown for 4 hr. Lane 3, DMSO treatment for 4 hr. Lane 4, ML3403 treatment for 4 hr.
Fig. 8 EgP38 phosphorylation in protoscolices cultivated with TGF-β1 in vitro. (A) Time-dependent phosphorylation of EgP38 following TGF-β1 treatment of protoscolices; immunoblotting was performed with either antibody as shown in Fig. 7. (B) Quantification by densitometry (n=4±SD; *P<0.01 compared the with 0 hr group).

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Molecular Cloning and Characterization of a P38-Like Mitogen-Activated Protein Kinase from Echinococcus granulosus
PHD : Parasites, Hosts and Diseases

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