Introduction (Background & Objectives) : Toxoplasma gondii, an intracellular apicomplexan parasite, poses significant health risks in both human and veterinary contexts globally. This study investigates the physicochemical and antigenic properties of the P30 protein (AAB21492.1) utilizing bioinformatics tools, aiming to evaluate its viability as a candidate for vaccine development and serological detection of T. gondii across diverse host species. Material & Methods : The antigenicity, allergenicity, and toxicity of the P30 protein were assessed using VaxiJen, AllerTop, and ToxinPred servers, respectively. The ProtParam server was employed to analyze the physicochemical characteristics of the protein. Additionally, linear B-cell and cytotoxic T lymphocyte (CTL) epitopes were predicted using the ABCpred webserver and the IEDB database, contributing to a comprehensive understanding of the protein's potential in immunological applications. Results : The analysis revealed that the P30 protein is antigenic, with a VaxiJen score of 0.7889, and is classified as non-allergenic and non-toxic. The physicochemical evaluation indicated a molecular weight of 34,761.71 Daltons. The instability index was calculated to be 37.55, suggesting favorable stability for vaccine formulation. The aliphatic index of 78.12 categorizes the protein as thermostable, while the theoretical isoelectric point (pI) was determined to be 7.89. The GRAVY index of 0.102 indicates a polar nature with significant water interaction, suggesting high solubility. Furthermore, the protein contains 23 negatively charged residues (Asp + Glu) and 25 positively charged residues (Arg + Lys), with a molecular formula of C1515H2434N410O481S21 and a total atom count of 4861. The QuerySol scaled solubility value was determined to be 0.336. Conclusion : Our findings also identified multiple linear B-cell and CTL epitopes within the P30 protein, all exhibiting high antigenicity, thereby underscoring their potential for use in vaccine development and serological detection of T. gondii.
