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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...

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Autores principales: Lee, Ho-Bin, Piao, Da-Chuan, Lee, Jun-Yeong, Choi, Jae-Yun, Bok, Jin-Duck, Cho, Chong-Su, Kang, Sang-Kee, Choi, Yun-Jaie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
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.
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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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