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Biological significance of phosphoenolpyruvate carboxykinase in a cestode parasite, Raillietina echinobothrida and effect of phytoestrogens on the enzyme from the parasite and its host, Gallus domesticus

Published online by Cambridge University Press:  09 May 2017

RAMNATH ,
ASIM KUMAR DUTTA ,
BARILIN DKHAR ,
VEENA TANDON  and
BIDYADHAR DAS
RAMNATH
Affiliation:
Department of Zoology, Biological Chemistry Laboratory, North-Eastern Hill University, Shillong-793022, Meghalaya, India
ASIM KUMAR DUTTA
Affiliation:
Department of Zoology, Biological Chemistry Laboratory, North-Eastern Hill University, Shillong-793022, Meghalaya, India
BARILIN DKHAR
Affiliation:
Department of Zoology, Biological Chemistry Laboratory, North-Eastern Hill University, Shillong-793022, Meghalaya, India
VEENA TANDON
Affiliation:
Biotech Park, Janki Puram Sector G, Kursi Road, Lucknow-226021, UP, India
BIDYADHAR DAS*
Affiliation:
Department of Zoology, Biological Chemistry Laboratory, North-Eastern Hill University, Shillong-793022, Meghalaya, India
*
*Corresponding author. Department of Zoology, Biological Chemistry Laboratory, North-Eastern Hill University, Shillong-793022, Meghalaya, India. E-mail: dasbidyadhar@gmail.com
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Summary

Phosphoenolpyruvate carboxykinase (PEPCK) is involved in glycolysis in the cestode parasite, Raillietina echinobothrida; whereas, it executes a gluconeogenic role in its host, Gallus domesticus. Because of its differing primary function in the cestode parasite and its host, this enzyme is regarded as a plausible anthelmintic target. Hence, the biological significance of PEPCK in the parasite was analysed using siRNA against PEPCK from R. echinobothrida (RePEPCK). In order to find out the functional differences between RePEPCK and GdPEPCK (PEPCK from its host, G. domesticus), PEPCK genes from both sources were cloned, over-expressed, characterized, and some properties of the purified enzymes were compared. RePEPCK and GdPEPCK showed a standard Michaelis-Menten kinetics with Kmapp of 46.9 and 22.9 µm, respectively, for phosphoenolpyruvate and Kmapp of 15.4 µm for oxaloacetate in GdPEPCK decarboxylation reaction. Here, we report antagonist behaviours of recombinant PEPCKs derived from the parasite and its host. In search of possible modulators for PEPCK, few phytoestrogens were examined on the purified enzymes and their inhibitory constants were determined and discussed. This study stresses the potential of these findings to validate PEPCK as the anthelmintic drug target for parasitism management.

Keywords

Gallus domesticusRaillietina echinobothridaPEPCKphytoestrogenssiRNA

Information

Type
Research Article
Information
Parasitology , Volume 144 , Issue 9 , August 2017 , pp. 1264 - 1274
Copyright
Copyright © Cambridge University Press 2017 

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