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Strong protection against ricin challenge induced by a novel modified ricin A-chain protein in mouse model
Ricin toxin (RT) is an extremely potent toxin derived from the castor bean plant. As a possible bioterrorist weapon, it was categorized as a level B agent in international society. With the growing awareness and concerns of the “white powder incident” in recent years, it is indispensable to develop...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4514271/ https://www.ncbi.nlm.nih.gov/pubmed/26038805 http://dx.doi.org/10.1080/21645515.2015.1038446 |
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author | Zhang, Tao Yang, Hao Kang, Lin Gao, Shan Xin, Wenwen Yao, Wenwu Zhuang, Xiangjin Ji, Bin Wang, Jinglin |
author_facet | Zhang, Tao Yang, Hao Kang, Lin Gao, Shan Xin, Wenwen Yao, Wenwu Zhuang, Xiangjin Ji, Bin Wang, Jinglin |
author_sort | Zhang, Tao |
collection | PubMed |
description | Ricin toxin (RT) is an extremely potent toxin derived from the castor bean plant. As a possible bioterrorist weapon, it was categorized as a level B agent in international society. With the growing awareness and concerns of the “white powder incident” in recent years, it is indispensable to develop an effective countermeasure against RT intoxication. In this study we used site-directed mutagenesis and polymerase chain reaction (PCR) techniques to modify the gene of ricin A-chain (RTA). As a result, we have generated a mutated and truncated ricin A-chain (mtRTA) vaccine antigen by E.coli strain. The cytotoxicity assay was used to evaluate the safety of the as-prepared mtRTA antigen, and the results showed that there was no residual toxicity observed when compared to the recombinant RTA (rRTA) or native RT. Furthermore, BALB/c mice were subcutaneously (s.c.) vaccinated with mtRTA 3 times at an interval of 2 weeks, and then the survivals were evaluated after intraperitoneal (i.p.) or intratracheal challenge of RT. The vaccinated mice developed a strong protective immune response that was wholly protective against 40 × LD(50) of RT i.p. injection or 20 × LD(50) of RT intratracheal spraying. The mtRTA antigen has great potential to be a vaccine candidate for future application in humans. |
format | Online Article Text |
id | pubmed-4514271 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-45142712016-02-03 Strong protection against ricin challenge induced by a novel modified ricin A-chain protein in mouse model Zhang, Tao Yang, Hao Kang, Lin Gao, Shan Xin, Wenwen Yao, Wenwu Zhuang, Xiangjin Ji, Bin Wang, Jinglin Hum Vaccin Immunother Research Paper Ricin toxin (RT) is an extremely potent toxin derived from the castor bean plant. As a possible bioterrorist weapon, it was categorized as a level B agent in international society. With the growing awareness and concerns of the “white powder incident” in recent years, it is indispensable to develop an effective countermeasure against RT intoxication. In this study we used site-directed mutagenesis and polymerase chain reaction (PCR) techniques to modify the gene of ricin A-chain (RTA). As a result, we have generated a mutated and truncated ricin A-chain (mtRTA) vaccine antigen by E.coli strain. The cytotoxicity assay was used to evaluate the safety of the as-prepared mtRTA antigen, and the results showed that there was no residual toxicity observed when compared to the recombinant RTA (rRTA) or native RT. Furthermore, BALB/c mice were subcutaneously (s.c.) vaccinated with mtRTA 3 times at an interval of 2 weeks, and then the survivals were evaluated after intraperitoneal (i.p.) or intratracheal challenge of RT. The vaccinated mice developed a strong protective immune response that was wholly protective against 40 × LD(50) of RT i.p. injection or 20 × LD(50) of RT intratracheal spraying. The mtRTA antigen has great potential to be a vaccine candidate for future application in humans. Taylor & Francis 2015-06-03 /pmc/articles/PMC4514271/ /pubmed/26038805 http://dx.doi.org/10.1080/21645515.2015.1038446 Text en © 2015 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted. |
spellingShingle | Research Paper Zhang, Tao Yang, Hao Kang, Lin Gao, Shan Xin, Wenwen Yao, Wenwu Zhuang, Xiangjin Ji, Bin Wang, Jinglin Strong protection against ricin challenge induced by a novel modified ricin A-chain protein in mouse model |
title | Strong protection against ricin challenge induced by a novel modified ricin A-chain protein in mouse model |
title_full | Strong protection against ricin challenge induced by a novel modified ricin A-chain protein in mouse model |
title_fullStr | Strong protection against ricin challenge induced by a novel modified ricin A-chain protein in mouse model |
title_full_unstemmed | Strong protection against ricin challenge induced by a novel modified ricin A-chain protein in mouse model |
title_short | Strong protection against ricin challenge induced by a novel modified ricin A-chain protein in mouse model |
title_sort | strong protection against ricin challenge induced by a novel modified ricin a-chain protein in mouse model |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4514271/ https://www.ncbi.nlm.nih.gov/pubmed/26038805 http://dx.doi.org/10.1080/21645515.2015.1038446 |
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