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A Novel Design of Multi-epitope Vaccine Against Helicobacter pylori by Immunoinformatics Approach
Helicobacter pylori (H. pylori) is a gram-negative spiral bacterium that caused infections in half of the world’s population and had been identified as type I carcinogen by the World Health Organization. Compared with antibiotic treatment which could result in drug resistance, the vaccine therapy is...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7778422/ https://www.ncbi.nlm.nih.gov/pubmed/33424523 http://dx.doi.org/10.1007/s10989-020-10148-x |
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author | Ma, Junfei Qiu, Jingxuan Wang, Shuying Ji, Qianyu Xu, Dongpo Wang, Haiwang Wu, Zhiguang Liu, Qing |
author_facet | Ma, Junfei Qiu, Jingxuan Wang, Shuying Ji, Qianyu Xu, Dongpo Wang, Haiwang Wu, Zhiguang Liu, Qing |
author_sort | Ma, Junfei |
collection | PubMed |
description | Helicobacter pylori (H. pylori) is a gram-negative spiral bacterium that caused infections in half of the world’s population and had been identified as type I carcinogen by the World Health Organization. Compared with antibiotic treatment which could result in drug resistance, the vaccine therapy is becoming a promising immunotherapy option against H. pylori. Further, the multi-epitope vaccine could provoke a wider immune protection to control H. pylori infection. In this study, the in-silico immunogenicity calculations on 381 protein sequences of H. pylori were performed, and the immunogenicity of selected proteins with top-ranked score were tested. The B cell epitopes and T cell epitopes from three well performed proteins UreB, PLA1, and Omp6 were assembled into six constructs of multi-epitope vaccines with random orders. In order to select the optimal constructs, the stability of the vaccine structure and the exposure of B cell epitopes on the vaccine surface were evaluated based on structure prediction and solvent accessible surface area analysis. Finally Construct S1 was selected and molecular docking showed that it had the potential of binding TLR2, TLR4, and TLR9 to stimulate strong immune response. In particular, this study provides good suggestions for epitope assembly in the construction of multi-epitope vaccines and it may be helpful to control H. pylori infection in the future. SUPPLEMENTARY INFORMATION: The online version of this article (10.1007/s10989-020-10148-x) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-7778422 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-77784222021-01-04 A Novel Design of Multi-epitope Vaccine Against Helicobacter pylori by Immunoinformatics Approach Ma, Junfei Qiu, Jingxuan Wang, Shuying Ji, Qianyu Xu, Dongpo Wang, Haiwang Wu, Zhiguang Liu, Qing Int J Pept Res Ther Article Helicobacter pylori (H. pylori) is a gram-negative spiral bacterium that caused infections in half of the world’s population and had been identified as type I carcinogen by the World Health Organization. Compared with antibiotic treatment which could result in drug resistance, the vaccine therapy is becoming a promising immunotherapy option against H. pylori. Further, the multi-epitope vaccine could provoke a wider immune protection to control H. pylori infection. In this study, the in-silico immunogenicity calculations on 381 protein sequences of H. pylori were performed, and the immunogenicity of selected proteins with top-ranked score were tested. The B cell epitopes and T cell epitopes from three well performed proteins UreB, PLA1, and Omp6 were assembled into six constructs of multi-epitope vaccines with random orders. In order to select the optimal constructs, the stability of the vaccine structure and the exposure of B cell epitopes on the vaccine surface were evaluated based on structure prediction and solvent accessible surface area analysis. Finally Construct S1 was selected and molecular docking showed that it had the potential of binding TLR2, TLR4, and TLR9 to stimulate strong immune response. In particular, this study provides good suggestions for epitope assembly in the construction of multi-epitope vaccines and it may be helpful to control H. pylori infection in the future. SUPPLEMENTARY INFORMATION: The online version of this article (10.1007/s10989-020-10148-x) contains supplementary material, which is available to authorized users. Springer Netherlands 2021-01-02 2021 /pmc/articles/PMC7778422/ /pubmed/33424523 http://dx.doi.org/10.1007/s10989-020-10148-x Text en © The Author(s), under exclusive licence to Springer Nature B.V. part of Springer Nature 2021 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Article Ma, Junfei Qiu, Jingxuan Wang, Shuying Ji, Qianyu Xu, Dongpo Wang, Haiwang Wu, Zhiguang Liu, Qing A Novel Design of Multi-epitope Vaccine Against Helicobacter pylori by Immunoinformatics Approach |
title | A Novel Design of Multi-epitope Vaccine Against Helicobacter pylori by Immunoinformatics Approach |
title_full | A Novel Design of Multi-epitope Vaccine Against Helicobacter pylori by Immunoinformatics Approach |
title_fullStr | A Novel Design of Multi-epitope Vaccine Against Helicobacter pylori by Immunoinformatics Approach |
title_full_unstemmed | A Novel Design of Multi-epitope Vaccine Against Helicobacter pylori by Immunoinformatics Approach |
title_short | A Novel Design of Multi-epitope Vaccine Against Helicobacter pylori by Immunoinformatics Approach |
title_sort | novel design of multi-epitope vaccine against helicobacter pylori by immunoinformatics approach |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7778422/ https://www.ncbi.nlm.nih.gov/pubmed/33424523 http://dx.doi.org/10.1007/s10989-020-10148-x |
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