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Bioinformatics analysis and construction of phylogenetic tree of aquaporins from Echinococcus granulosus

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Abstract

Cyst echinococcosis caused by the matacestodal larvae of Echinococcus granulosus (Eg), is a chronic, worldwide, and severe zoonotic parasitosis. The treatment of cyst echinococcosis is still difficult since surgery cannot fit the needs of all patients, and drugs can lead to serious adverse events as well as resistance. The screen of target proteins interacted with new anti-hydatidosis drugs is urgently needed to meet the prevailing challenges. Here, we analyzed the sequences and structure properties, and constructed a phylogenetic tree by bioinformatics methods. The MIP family signature and Protein kinase C phosphorylation sites were predicted in all nine EgAQPs. α-helix and random coil were the main secondary structures of EgAQPs. The numbers of transmembrane regions were three to six, which indicated that EgAQPs contained multiple hydrophobic regions. A neighbor-joining tree indicated that EgAQPs were divided into two branches, seven EgAQPs formed a clade with AQP1 from human, a “strict” aquaporins, other two EgAQPs formed a clade with AQP9 from human, an aquaglyceroporins. Unfortunately, homology modeling of EgAQPs was aborted. These results provide a foundation for understanding and researches of the biological function of E. granulosus.

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References

  • Beitz E (2005) Aquaporins from pathogenic protozoan parasites: structure, function and potential for chemotherapy. Biol Cell 6:373–383

    Article  Google Scholar 

  • Beitz E, Golldack A, Rothert M, Bülow JV (2015) Challenges and achievements in the therapeutic modulation of aquaporin functionality. Pharmacol Ther 155:22–35

    Article  CAS  PubMed  Google Scholar 

  • Benga G (2012) On the definition, nomenclature and classification of water channel proteins (aquaporins and relatives). Mol Aspects Med 33:514–517

    Article  CAS  PubMed  Google Scholar 

  • Bordoli L, Kiefer F, Arnold K, Benkert P, Battey J, Schwede T (2009) Protein structure homology modeling using SWISS-MODEL workspace. Nat Protoc 4:1–13

    Article  CAS  PubMed  Google Scholar 

  • Chaumont F, Moshelion M, Daniels MJ (2005) Regulation of plant aquaporin activity. Biol Cell 97:749–764

    Article  CAS  PubMed  Google Scholar 

  • Geadkaew A, Bulow JV, Beitz E, Grams SV, Viyanant V, Grams R (2011) Functional analysis of novel aquaporins from Fasciola gigantaca. Mol Biochem Parastitol 2:144–153

    Article  Google Scholar 

  • Gowder SM, Chatterjee J, Chaudhuri T, Paul K (2014) Prediction and analysis of surface hydrophobic residues in tertiary structure of proteins. Sci Word J 071258

  • Hansen M, Kun JF, Schultz JE, Beitz E (2002) A single, bi-functional aquaglyceroporin in blood stage Plasmodium falciparum malaria parasites. J Biol Chem 7:4874–4882

    Article  Google Scholar 

  • Hemphill A, Stadelmann B, Rufener R, Spiliotis M, Boubaker G, Muller J, Muller N, Gorgas D, Gottstern B (2014) Treatment of echinococcosis: albendazole and menbendazole—what else? Parasite 21:1–9

    Article  Google Scholar 

  • Kazutoshi T, Yoshinori F (2014) Water channel structures analysed by electron crystallography. Biochim Biophys Acta 1840:1605–1613

    Article  Google Scholar 

  • Kitchen P, Day RE, Salman MM, Conner MT, Bill RM, Conner AC (2015) Beyond water homeoatasis: diverse functional roles of mammalian aquaporins. Biochimica et Biophysica 12:2410–2421

    Article  Google Scholar 

  • Perticaroli S, Nickels JD, Ehlers G, Sokolov AP (2014) Rigidity, secondary structure, and the universality of the Boson Peak in proteins. Biophys J 106:2667–2674

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Song J (2014) Parasite aquaporins: current developments in drug facilitation and resistance. Biochim Biophys Acta 1840:1566–1573

    Article  CAS  PubMed  Google Scholar 

  • Song J, He QF (2012) Bioinformatics analysis of the structure and linear B-cell epitopes of aquaporin-3 from Schistosoma japonicum. Asian Pac J Trop Med 2:107–109

    Article  Google Scholar 

  • Zhang NZ, Huang SY, Zhou DH, Xu Y, He JJ, Zhu XQ (2014) Identification and bioinformatic analysis of a putative calcium-dependent protein kinase (CDPK6) from Toxoplasma gondii. Genet Mol Res 4:10677–10699

    Google Scholar 

Download references

Acknowledgments

This study was funded by the National Natural Science Foundation of China (grant numbers 30972567 and 30371258).

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Correspondence to Bin Ye.

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Wang, F., Ye, B. Bioinformatics analysis and construction of phylogenetic tree of aquaporins from Echinococcus granulosus . Parasitol Res 115, 3499–3511 (2016). https://doi.org/10.1007/s00436-016-5114-2

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  • DOI: https://doi.org/10.1007/s00436-016-5114-2

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