In silico design of a chimeric protein containing antigenic fragments of Helicobacter pylori; A bioinformatic approach

Mohammad, N. and Karsabet, M.T. and Amani, J. and Ardjmand, A. and Razavizadeh, M. and khalifeh-Gholi, M. and Saffari, M. and Ghasemi, A. (2016) In silico design of a chimeric protein containing antigenic fragments of Helicobacter pylori; A bioinformatic approach. Open Microbiology Journal, 10. pp. 97-112.

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Abstract

Helicobacter pylori is a global health problem which has encouraged scientists to find new ways to diagnose, immunize and eradicate the H. pylori infection. In silico studies are a promising approach to design new chimeric antigen having the immunogenic potential of several antigens. In order to obtain such benefit in H. pylori vaccine study, a chimeric gene containing four fragments of FliD sequence (1-600 bp), UreB (327-334 bp),VacA (744-805 bp) and CagL(51-100 bp) which have a high density of B- and T-cell epitopes was designed. The secondary and tertiary structures of the chimeric protein and other properties such as stability, solubility and antigenicity were analyzed. The in silico results showed that after optimizing for the purpose of expression in Escherichia coli BL21, the solubility and antigenicity of the construct fragments were highly retained. Most regions of the chimeric protein were found to have a high antigenic propensity and surface accessibility. These results would be useful in animal model application and accounted for the development of an epitope-based vaccine against the H. pylori. © Mohammad et al..

Item Type: Article
Additional Information: cited By 1
Uncontrolled Keywords: bacterial protein; CagL protein; chimeric protein; epitope; protein FliD; unclassified drug; vacuolating toxin, Article; B lymphocyte; bioinformatics; codon usage; computer model; gene expression; Helicobacter pylori; hydrophobicity; immunogenicity; nonhuman; physical chemistry; priority journal; protein conformation; protein secondary structure; protein stability; protein tertiary structure; sequence alignment; sequence analysis; T lymphocyte; translation initiation
Subjects: Immunology and Microbiology
Divisions: Faculty of Medicine > Basic Sciences > Department of Microbiology & Immunology
Depositing User: editor . 2
Date Deposited: 08 Mar 2017 22:36
Last Modified: 08 Mar 2017 22:36
URI: http://eprints.kaums.ac.ir/id/eprint/150

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