Bioinformatic prediction of the epitopes of Echinococcus granulosus antigen 5

Pan,Wei; Chen,De‑Sheng; Lu,Yun‑Juan; Sun,Fen‑Fen; Xu,Hui‑Wen; Zhang,Ya‑Wen; Yan,Chao; Fu,Lin‑Lin; Zheng,Kui‑Yang; Tang,Ren‑Xian

doi:10.3892/br.2016.827

Bioinformatic prediction of the epitopes of Echinococcus granulosus antigen 5

Authors:
- Wei Pan
- De‑Sheng Chen
- Yun‑Juan Lu
- Fen‑Fen Sun
- Hui‑Wen Xu
- Ya‑Wen Zhang
- Chao Yan
- Lin‑Lin Fu
- Kui‑Yang Zheng
- Ren‑Xian Tang
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Affiliations: Department of Pathogenic Biology and Immunology, Laboratory of Infection and Immunity, Xuzhou, Jiangsu 221004, P.R. China
Published online on: December 9, 2016 https://doi.org/10.3892/br.2016.827
Pages: 181-187
Copyright: © Pan et al. This is an open access article distributed under the terms of Creative Commons Attribution License.

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Abstract

The aim of the present study was to predict and analyze the secondary structure, and B and T cell epitopes of Echinococcus granulosus antigen 5 (Ag5) using online software in order to investigate its immunogenicity and preliminarily evaluate its potential as an effective antigen peptide vaccine for cystic echinococcosis. The PortParam program was used to analyze molecular weight, the theoretical isoelectric point, instability index and other physicochemical properties. The secondary structure of the Ag5 protein was predicted using Self‑Optimized Prediction method With Alignment and the tertiary structure of the Ag5 protein was predicted using 3DLigandSite together with Center for Biological Sequence Analysis Prediction Servers. Furthermore, the Immune Epitope Database software was used to predict B cell epitopes, and T cell epitopes were predicted with the BioInformatics and Molecular Analysis Section and SYFPEITHI programs. The results demonstrated that α‑helixes, β‑turns, random coils and extended strands account for 23.35, 10.95, 41.32, and 24.38% of the secondary structure of the Ag5 protein, respectively. Ten potential B cell epitopes of Ag5 were identified as the amino acids sequences 27‑39, 70‑80, 117‑130, 146‑168, 250‑262, 284‑293, 339‑349, 359‑371, 403‑412 and 454‑462, and seven potential T cell epitopes were identified as the amino acid sequences 52‑60, 57‑65, 182‑190, 231‑239, 273‑281, 318‑326 and 467‑475. Thus, ten B cell epitopes and seven T cell epitopes were identified on Ag5, suggesting the strong immunogenicity of this protein, which could be applied to design antigen peptide vaccines for echinococcosis.

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