Pencirian molekul glikogen sintase kinase-3 Dari Eimeria tenella

Translated title of the contribution: Molecular characterisation of glycogen synthase kinase-3 from Eimeria tenella

Ping Ping Yao, Mohd Firdaus Mohd Raih, Hasidah Mohd. Sidek, Mohammed Noor Embi, Kiew Lian Wan

Research output: Contribution to journalArticle

Abstract

The discovery of new anticoccidial drug targets is amongst the necessary efforts needed to control chicken coccidiosis caused by Eimeria species. In this study, the fragment coding for the putative Eimeria tenella glycogen synthase kinase-3 (GSK-3) was amplified from the cDNA of E. tenella. Homology search showed that generated E. tenella GSK-3 sequence has high similarities with GSK-3 sequences from other organisms. The conserved domains of GSK-3 and residues important for the GSK-3 activity were also predicted within the E. tenella GSK-3. Secondary structure analysis and homology modelling predicted that the protein structure is divided into a beta strand domain at the N terminal and an alpha helix domain at terminal C, which are characteristics of GSK-3 enzymes. These results supported the E. tenella GSK-3 codes for the GSK-3 protein in E. tenella. Although the degree of conservation is high, significant differences were observed between GSK-3 of E. tenella and its host. The Ser 9 residue reported to be important for the inhibition of the GSK-3 activity was not conserved within the E. tenella GSK-3. Considering that Ser 9 is a phosphorylation site in GSK-3β of vertebrates, the absence of this residue in the E. tenella GSK-3 sequence suggests that the regulation of E. tenella GSK-3 involves a different phosphorylation site and mechanism. Phylogenetic analysis suggests that E. tenella GSK-3 has a closer relationship to plant GSK-3. Superposition analysis between E. tenella GSK-3 and Homo sapiens GSK-3β predicted that E. tenella GSK-3 is able to interact with a GSK-3 inhibitor. Taken together, these results suggested that the E. tenella GSK-3 has the potential to be developed into an anticoccidial drug target.

Original languageIndonesian
Pages (from-to)1947-1957
Number of pages11
JournalSains Malaysiana
Volume45
Issue number12
Publication statusPublished - 1 Dec 2016

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Eimeria tenella
tau-protein kinase
coccidiostats
phosphorylation

Keywords

  • Anti-coccidial drug target
  • Coccidiosis
  • Protozoan parasite

ASJC Scopus subject areas

  • General

Cite this

Pencirian molekul glikogen sintase kinase-3 Dari Eimeria tenella. / Yao, Ping Ping; Mohd Raih, Mohd Firdaus; Mohd. Sidek, Hasidah; Embi, Mohammed Noor; Wan, Kiew Lian.

In: Sains Malaysiana, Vol. 45, No. 12, 01.12.2016, p. 1947-1957.

Research output: Contribution to journalArticle

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AB - The discovery of new anticoccidial drug targets is amongst the necessary efforts needed to control chicken coccidiosis caused by Eimeria species. In this study, the fragment coding for the putative Eimeria tenella glycogen synthase kinase-3 (GSK-3) was amplified from the cDNA of E. tenella. Homology search showed that generated E. tenella GSK-3 sequence has high similarities with GSK-3 sequences from other organisms. The conserved domains of GSK-3 and residues important for the GSK-3 activity were also predicted within the E. tenella GSK-3. Secondary structure analysis and homology modelling predicted that the protein structure is divided into a beta strand domain at the N terminal and an alpha helix domain at terminal C, which are characteristics of GSK-3 enzymes. These results supported the E. tenella GSK-3 codes for the GSK-3 protein in E. tenella. Although the degree of conservation is high, significant differences were observed between GSK-3 of E. tenella and its host. The Ser 9 residue reported to be important for the inhibition of the GSK-3 activity was not conserved within the E. tenella GSK-3. Considering that Ser 9 is a phosphorylation site in GSK-3β of vertebrates, the absence of this residue in the E. tenella GSK-3 sequence suggests that the regulation of E. tenella GSK-3 involves a different phosphorylation site and mechanism. Phylogenetic analysis suggests that E. tenella GSK-3 has a closer relationship to plant GSK-3. Superposition analysis between E. tenella GSK-3 and Homo sapiens GSK-3β predicted that E. tenella GSK-3 is able to interact with a GSK-3 inhibitor. Taken together, these results suggested that the E. tenella GSK-3 has the potential to be developed into an anticoccidial drug target.

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