Determining a multi-epitope vaccine of EgTeg protein using immuno-informatics approach

Abstract

Background: The results of studies using immuno-informatic tools and molecular modeling methods to predict and detect Echinococcus granulosus antigen epitopes and to design multi-epitope vaccines containing B and T cell epitopes are being studied. Therefore, it is time and economically advantageous to develop a peptide vaccine model predicted by the immuno-informatic model of multi-epitopes vaccines using the Echinococcus granulosus antigen nucleotide sequence. Aim: To develop a possible model of a multi-epitope vaccine against Echinococcus granulosus. Materials and Methods: To determine the amino acid sequence of the EgTeg protein, a searching by GenBank, the physicochemical parameters were processed by Expasy software, transmembrane domain and protein signal peptide information was processed by TMHMM online server, and EgTeg protein phosphorylation was used by NetPhos3.1 online server. Sopma and swiss-model online programs were used to determine the three dimensional structure of the protein, and the B-cell epitope was developed using the IEDB and I-TASSER online programs to develop a three-dimensional structure of the vaccine. Results: EgTeg protein consists of 105 amino acid residues with a total number of atoms are 1705, a molecular structure is C547H848N142O165S3, and a molecular weight are 12 kDa. Testing of the EgTeg protein on the TMHMM online server revealed that between 65 and 87 of the amino acid sequences were transmembrane domains. The secondary structure of the EgTeg protein was determined by alpha helix (Hh) 36.54%, Extended strand (Ee) 23.08%, Beta turn (Tt) 8.65%, and Random coil (Cc) 31.73% of the total amino acid sequence in the Sopma online application. Conclusion: EgTeg protein amino acid sequence, total atomic number, molecular structure, molecular weight, theoretical pI, Instability index (II), Aliphatic index, Grand average hydropathicity (GRAVY), domain location, and secondary structure information were determined. A possible model of a multi-epitope vaccine against Echinococcus granulosus was identified by the EgTeg protein B cell epitope (TMSRSEVEVLKSDMPTEM EYNADSSRPIKL) –GGSSGG linker protein and the three-dimensional structure of the vaccine was predicted.