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Artificially designed recombinant protein composed of multiple epitopes of foot-and-mouth disease virus as a vaccine candidate
BACKGROUND: Concerns regarding the safety of inactivated foot-and-mouth disease (FMD) vaccine have been raised since it is produced from cultured live FMD virus (FMDV). To overcome this issue, recombinant protein has been studied as an alternative vaccine. RESULTS AND CONCLUSION: We designed a chime...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5322615/ https://www.ncbi.nlm.nih.gov/pubmed/28228147 http://dx.doi.org/10.1186/s12934-017-0648-2 |
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author | Lee, Ho-Bin Piao, Da-Chuan Lee, Jun-Yeong Choi, Jae-Yun Bok, Jin-Duck Cho, Chong-Su Kang, Sang-Kee Choi, Yun-Jaie |
author_facet | Lee, Ho-Bin Piao, Da-Chuan Lee, Jun-Yeong Choi, Jae-Yun Bok, Jin-Duck Cho, Chong-Su Kang, Sang-Kee Choi, Yun-Jaie |
author_sort | Lee, Ho-Bin |
collection | PubMed |
description | BACKGROUND: Concerns regarding the safety of inactivated foot-and-mouth disease (FMD) vaccine have been raised since it is produced from cultured live FMD virus (FMDV). To overcome this issue, recombinant protein has been studied as an alternative vaccine. RESULTS AND CONCLUSION: We designed a chimerical multi-epitope recombinant protein (5BT), which is comprised of tandem repeats of five B cell epitopes (residue of VP1 136–162) derived from different FMDV variants and one T-cell epitope (residue of 3A 21–35). To increase solubility and stability of 5BT, it was conjugated with BmpB, the membrane protein B of Brachyspira hyodysenteriae (B5BT). Our results indicated that 5BT was susceptible to degradation by host protease and produced with substantial fraction of inclusion body. The stability and solubility of 5BT was greatly increased by conjugating to BmpB. FMDV specific antibodies were observed in the serum of mice immunized with 5BT and B5BT comparable to inactivated FMD vaccine. Sera from 5BT and B5BT groups also exhibited high epitope-specific antibody titers in peptide specific ELISA, indicating that all five epitopes are exposed to the B cell receptor for the antibody reaction. Thus the multi-epitope recombinant protein designed in this study may be a potential candidate as an alternative vaccine against FMDV epidemic variants. |
format | Online Article Text |
id | pubmed-5322615 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-53226152017-03-01 Artificially designed recombinant protein composed of multiple epitopes of foot-and-mouth disease virus as a vaccine candidate Lee, Ho-Bin Piao, Da-Chuan Lee, Jun-Yeong Choi, Jae-Yun Bok, Jin-Duck Cho, Chong-Su Kang, Sang-Kee Choi, Yun-Jaie Microb Cell Fact Research BACKGROUND: Concerns regarding the safety of inactivated foot-and-mouth disease (FMD) vaccine have been raised since it is produced from cultured live FMD virus (FMDV). To overcome this issue, recombinant protein has been studied as an alternative vaccine. RESULTS AND CONCLUSION: We designed a chimerical multi-epitope recombinant protein (5BT), which is comprised of tandem repeats of five B cell epitopes (residue of VP1 136–162) derived from different FMDV variants and one T-cell epitope (residue of 3A 21–35). To increase solubility and stability of 5BT, it was conjugated with BmpB, the membrane protein B of Brachyspira hyodysenteriae (B5BT). Our results indicated that 5BT was susceptible to degradation by host protease and produced with substantial fraction of inclusion body. The stability and solubility of 5BT was greatly increased by conjugating to BmpB. FMDV specific antibodies were observed in the serum of mice immunized with 5BT and B5BT comparable to inactivated FMD vaccine. Sera from 5BT and B5BT groups also exhibited high epitope-specific antibody titers in peptide specific ELISA, indicating that all five epitopes are exposed to the B cell receptor for the antibody reaction. Thus the multi-epitope recombinant protein designed in this study may be a potential candidate as an alternative vaccine against FMDV epidemic variants. BioMed Central 2017-02-22 /pmc/articles/PMC5322615/ /pubmed/28228147 http://dx.doi.org/10.1186/s12934-017-0648-2 Text en © The Author(s) 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Lee, Ho-Bin Piao, Da-Chuan Lee, Jun-Yeong Choi, Jae-Yun Bok, Jin-Duck Cho, Chong-Su Kang, Sang-Kee Choi, Yun-Jaie Artificially designed recombinant protein composed of multiple epitopes of foot-and-mouth disease virus as a vaccine candidate |
title | Artificially designed recombinant protein composed of multiple epitopes of foot-and-mouth disease virus as a vaccine candidate |
title_full | Artificially designed recombinant protein composed of multiple epitopes of foot-and-mouth disease virus as a vaccine candidate |
title_fullStr | Artificially designed recombinant protein composed of multiple epitopes of foot-and-mouth disease virus as a vaccine candidate |
title_full_unstemmed | Artificially designed recombinant protein composed of multiple epitopes of foot-and-mouth disease virus as a vaccine candidate |
title_short | Artificially designed recombinant protein composed of multiple epitopes of foot-and-mouth disease virus as a vaccine candidate |
title_sort | artificially designed recombinant protein composed of multiple epitopes of foot-and-mouth disease virus as a vaccine candidate |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5322615/ https://www.ncbi.nlm.nih.gov/pubmed/28228147 http://dx.doi.org/10.1186/s12934-017-0648-2 |
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