Find in Library

Vaccination is a prominent strategy to confine cystic echinococcosis (CE) in areas of endemicity worldwide. The present study was performed to predict the primary biochemical features and immunogenic epitopes of Echinococcus granulosus cyclophilin protein as a potential vaccine candidate. 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 162-residue, 17.35 kDa molecule, with relative thermotolerance (aliphatic: 60.12) and hydrophilicity (negative GRAVY). There were N-glycosylation and phosphorylation sites in the sequence, without a transmembrane domain. Moreover, several B-cell, MHC-binding and CTL epitopes were found in the EgGST protein, which could be further used in multi-epitope vaccines. In conclusion, the protein and its epitopes should be examined in wet lab experiments and in vivo.