Abstract
Clinostomum is a fish-borne pathogen,digenetic trematode with worldwide distribution. Despite its zoonootic significance, the molecules involved in the host-parasite interaction remains unknown. The present study deals with the proteome profile of the rDNA of Clinostomum piscidium using in silico workflow.The physicochemical properties, mass spectrometry ,atomic composition,estimated half-life in different hosts ,Grand average of hydropathy (GRAVY),extinction coefficient and instability index of the rDNA was studied.We identified hypothetical proteins(polar in nature) that showed similarities with proteins of Trichellina pseudospiralis and Melampsora laricipopulina.The functionality of these proteins revealed their role in intracellular signalling as a substrate for O - linked N - acetylglucosaminetransferases and death transcription factor(DIDO-1). This is the first report of our findings that aims to provide a better understanding of the mechanism by which this digenetic trematode adapts to extreme environments. It is expected that this study will lead to new insights into drug designing strategies and disease control.
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