biochemical properties and immunogenic epitopes of echinococcus granulosus glutathione s-transferase as a vaccine target: in-silico study

Background: the current in silico study was done to determine the primary biochemical features and immunogenic epitopes of echinococcus granulosus glutathione s-transferase protein as a potential vaccine candidate.methods: several web tools were employed to predict physico-chemical properties, antigenicity, allergenicity, solubility, post-translational modification (ptm) sites, subcellular localization, signal peptide, transmembrane domain, secondary and tertiary structure followed by refinement and validations. in addition, b-cell epitopes were predicted and were screened using various web servers, while mhc-binding and ctl epitopes were predicted using iedb and netctl servers, respectively.results: the protein had 219 residues with a molecular weight of 25.55 kda and alkaline isoelectric ph (7.5). this protein was stable, thermotolerant (aliphatic index: 78.04) and hydrophilic (gravy: -0.440). the predicted antigenicity scores were low and the protein was non-allergenic in nature. there were no transmembrane domain and signal peptide in the sequence. moreover, several b-cell, mhc-binding and ctl epitopes were found in the eggst protein, which could be further used in multi-epitope vaccines.conclusion: further studies are needed on the development of vaccines in vivo using eggst alone or in combination with other antigens in the future.