Introduction (Background & Objectives) : Cystic echinococcosis, or hydatid disease, causes cysts usually in the liver and lungs. Designing effective vaccines and finding suitable proteins for serological detection are crucial for combating cystic echinococcosis. In this study the physicochemical and antigenic properties of the EPC1 protein (AOY34842.1) were evaluated utilizing bioinformatics tools, in order to evaluate its viability as a candidate for vaccine development and serological detection of Echinococcus granulosus across diverse host species. Material & Methods : The antigenicity, allergenicity, and toxicity of the EPC1 protein were evaluated using VaxiJen, AllerTop, and ToxinPred servers, respectively, to assess its suitability for immunological applications. The physicochemical properties of the protein were analyzed using the ProtParam server. Furthermore, linear B-cell epitopes were predicted with the ABCpred webserver, while cytotoxic T lymphocyte (CTL) epitopes were identified using the IEDB database. These analyses provide a comprehensive understanding of the potential of the EPC1 protein as a candidate for vaccine development and serological detection against E. granulosus across diverse host species. Results : The analysis indicated that the EPC1 protein is antigenic, with a VaxiJen score of 0.6147, and is classified as non-allergenic and non-toxic. The physicochemical evaluation revealed a molecular weight of 20,039.89 Daltons and an estimated half-life of 30 hours in mammalian reticulocytes in vitro, over 20 hours in yeast in vivo, and more than 10 hours in Escherichia coli in vivo. An aliphatic index of 80.69 categorizes the protein as thermostable, while the theoretical isoelectric point (pI) was determined to be 7.00. The GRAVY index of -0.506 indicates a polar nature with favorable water interaction, suggesting high solubility. Additionally, the protein comprises 26 negatively charged residues (aspartic acid and glutamic acid) and 26 positively charged residues (arginine and lysine), with a molecular formula of C884H1403N245O268S9 and a total atom count of 2809. The QuerySol scaled solubility value was calculated to be 0.541. Conclusion : Furthermore, our findings identified multiple linear B-cell and cytotoxic T lymphocyte (CTL) epitopes within the EPC1 protein, all demonstrating high antigenicity, thereby highlighting their potential for application in vaccine development and serological detection of E. granulosus.
