| Popis: |
Vaccination can be a key step in controlling hydatid cyst infection in humans and livestock in endemic areas of the disease. The aim of the Present study was to determine some of the basal biochemical properties followed by prediction and screening of B-cell and MHC-binding epitopes of EgP29 protein in silico. Some of the basic physico-chemical properties along with antigenicity, allergenicity, solubility, post-translational modification (PTM) sites, subcellular localization, signal peptide, transmembrane domain, secondary and tertiary structures followed by refinement and validations were computationally determined for this protein. Also, B-cell epitopes were predicted and screened using various web servers, while MHC-binding and CTL epitopes were predicted using IEDB and NetCTL servers, respectively. The protein is a 238-residue, 27 kDa molecule, with high thermotolerance (aliphatic: 71.81) and hydrophilicity (negative GRAVY). There were several glycosylation and phosphorylation sites in the sequence, without a transmembrane domain and signal peptide. Moreover, several B-cell and MHC-binding epitopes were found in the EgP29 protein, which could be further used in multi-epitope vaccines. In conclusion, results of the present study can be a promising sign for achieving effective approaches to the preparation of a multi-epitope vaccines against echinococcosis. So, it is necessary that the effectiveness of the protein and its epitopes be evaluated in vitro and in vivo. |
