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Research Paper | Zoology | India | Volume 4 Issue 6, June 2015
Effect of Adhatoda vasica and Piper Betle Leaves Extracts on Motility and Acetylcholinesterase of Cotylophoron Cotylophorum Invitro
Jeya S [2] | Veerakumari L
Abstract: Parasitism by gastrointestinal trematodes is one of the major constraints on livestock production all over the world. Paramphistomosis is commonly known as stomach fluke disease, caused by infestation of ruminants with paramphistome species. Cotylophoron cotylophorum is one among the paramphistome species, which cause the disease Paramphistomosis. The clinical symptoms of this disease include weight loss, loss of production and anemia, immature flukes cause diarrhoea in sheep and goats. The current scenario of plant based drugs for various ailments of human beings as well livestock instigated us to carry out the present study which is a sincere attempt to reveal the anthelmintic activity of solvent extracts of Adhatoda vasica (Av) and Piper betle (Pb) leaves against C. cotylophorum. Motility and acetylcholinesterase (AChE) are taken as biomarkers to identify the anthelmintic efficacy of Av and Pb. Gross visual observations of motility of the parasites against various solvent extracts revealed that the ethyl acetate extract of both plants (AvEaE, PbEaE) were effective. The flukes were exposed to five different sub lethal concentrations of AvEaE and PbEaE (0.01, 0.05, 0.1, 0.5 and 1.0mg/ml) for 2h, 4h and 8h. Highest percentage of inhibition in motility and AChE was found in drug treated parasites after 8 h of exposure. AChE is an important enzyme in helminths which is associated with the neuromuscular coordination. The inhibition of AChE could be the significant reason for the drastic changes in motility of the parasites. Results of this study clearly showed that the extracts of AvEaE and PbEaE had immolated the parasites by affecting their neurotransmission and dismantle the muscular coordination system.
Keywords: Paramphistomosis, Cotylophoron cotylophorum, Adhatoda vasica, Piper betle, Acetylcholinesterase
Edition: Volume 4 Issue 6, June 2015,
Pages: 1556 - 1561