In silico analysis of a Skp1 protein homolog from the human pathogen E. histolytica

In this study, we have presented the first comprehensive analysis of the presence of peptides or proteins in the human pathogenEntamoeba histolytica having homology to Skp1protein. The occurrence of other protein components of the SCF complex has been identified from protein –protein interaction network of EhSkp1A. Studying the role of Skp1protein in this pathogen would help to understand its unique chromosome segregation and cell division which are different from higher eukaryotes. Further, owing to the development of resistance over several drugs that are currently available, there is a growing need for a novel drug againstE. histolytica. Proteins from ubiquitin-proteasome pathway have received attention as potential drug targets in other parasites. We have identified four homologs of Skp1 protein inE. histolytica strain HM-1: IMSS. Molecular docking study between EhSkp1A and an F-box/WD domain-containing protein (EhFBXW) shows that the F-box domain in the N-terminal region of EhFBXW interacts with EhSkp1A. Therefore, the results of the present study shall provide a stable foundation for further research on the cell cycle regulation ofE. histolytica and this will help researchers to develop new drugs against this parasite.
Source: Journal of Parasitic Diseases - Category: Parasitology Source Type: research