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Unique Epitopes Recognized by Monoclonal Antibodies against HP-PRRSV: Deep Understanding of Antigenic Structure and Virus-Antibody Interaction
Highly pathogenic porcine reproductive and respiratory syndrome virus (HP-PRRSV) is a member of the genus Arterivirus within the family Arteriviridae. N and GP3 proteins are the immunodominance regions of the PRRSV viral proteins. To identify the B-cell linear antigenic epitopes within HP-PRRSV N an...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4216098/ https://www.ncbi.nlm.nih.gov/pubmed/25360600 http://dx.doi.org/10.1371/journal.pone.0111633 |
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author | Wang, Qian Peng, Jinmei Sun, Yan Chen, Jiazeng An, Tongqing Leng, Chaoliang Li, Lin Zhao, Hongyuan Guo, Xin Ge, Xinna Yang, Hanchun Tian, Zhijun |
author_facet | Wang, Qian Peng, Jinmei Sun, Yan Chen, Jiazeng An, Tongqing Leng, Chaoliang Li, Lin Zhao, Hongyuan Guo, Xin Ge, Xinna Yang, Hanchun Tian, Zhijun |
author_sort | Wang, Qian |
collection | PubMed |
description | Highly pathogenic porcine reproductive and respiratory syndrome virus (HP-PRRSV) is a member of the genus Arterivirus within the family Arteriviridae. N and GP3 proteins are the immunodominance regions of the PRRSV viral proteins. To identify the B-cell linear antigenic epitopes within HP-PRRSV N and GP3 proteins, two monoclonal antibodies (mAbs) against N and GP3 proteins were generated and characterized, designated as 3D7 and 1F10 respectively. The mAb 3D7 recognized only HuN4-F112 not the corresponding virulent strain (HuN4-F5). It also recognized two other commercial vaccines (JXA1-R and TJM-F92), but not two other HP-PRRSV strains (HNZJJ-F1 and HLJMZ-F2). The B-cell epitope recognized by the mAb 3D7 was localized to N protein amino acids 7–33. Western blot showed that the only difference amino acid between HuN4-F112-N and HuN4-F5-N did not change the mAb 3D7 recognization to N protein. The epitope targeted by the mAb 1F10 was mapped by truncated proteins. We found a new epitope (68-76aa) can be recognized by the mAb. However, the epitope could not be recognized by the positive sera, suggesting the epitope could not induce antibody in pigs. These results should extend our understanding of the antigenic structure of the N protein and antigen-antibody reactions of the GP3 protein in different species. |
format | Online Article Text |
id | pubmed-4216098 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-42160982014-11-05 Unique Epitopes Recognized by Monoclonal Antibodies against HP-PRRSV: Deep Understanding of Antigenic Structure and Virus-Antibody Interaction Wang, Qian Peng, Jinmei Sun, Yan Chen, Jiazeng An, Tongqing Leng, Chaoliang Li, Lin Zhao, Hongyuan Guo, Xin Ge, Xinna Yang, Hanchun Tian, Zhijun PLoS One Research Article Highly pathogenic porcine reproductive and respiratory syndrome virus (HP-PRRSV) is a member of the genus Arterivirus within the family Arteriviridae. N and GP3 proteins are the immunodominance regions of the PRRSV viral proteins. To identify the B-cell linear antigenic epitopes within HP-PRRSV N and GP3 proteins, two monoclonal antibodies (mAbs) against N and GP3 proteins were generated and characterized, designated as 3D7 and 1F10 respectively. The mAb 3D7 recognized only HuN4-F112 not the corresponding virulent strain (HuN4-F5). It also recognized two other commercial vaccines (JXA1-R and TJM-F92), but not two other HP-PRRSV strains (HNZJJ-F1 and HLJMZ-F2). The B-cell epitope recognized by the mAb 3D7 was localized to N protein amino acids 7–33. Western blot showed that the only difference amino acid between HuN4-F112-N and HuN4-F5-N did not change the mAb 3D7 recognization to N protein. The epitope targeted by the mAb 1F10 was mapped by truncated proteins. We found a new epitope (68-76aa) can be recognized by the mAb. However, the epitope could not be recognized by the positive sera, suggesting the epitope could not induce antibody in pigs. These results should extend our understanding of the antigenic structure of the N protein and antigen-antibody reactions of the GP3 protein in different species. Public Library of Science 2014-10-31 /pmc/articles/PMC4216098/ /pubmed/25360600 http://dx.doi.org/10.1371/journal.pone.0111633 Text en © 2014 Wang et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Wang, Qian Peng, Jinmei Sun, Yan Chen, Jiazeng An, Tongqing Leng, Chaoliang Li, Lin Zhao, Hongyuan Guo, Xin Ge, Xinna Yang, Hanchun Tian, Zhijun Unique Epitopes Recognized by Monoclonal Antibodies against HP-PRRSV: Deep Understanding of Antigenic Structure and Virus-Antibody Interaction |
title | Unique Epitopes Recognized by Monoclonal Antibodies against HP-PRRSV: Deep Understanding of Antigenic Structure and Virus-Antibody Interaction |
title_full | Unique Epitopes Recognized by Monoclonal Antibodies against HP-PRRSV: Deep Understanding of Antigenic Structure and Virus-Antibody Interaction |
title_fullStr | Unique Epitopes Recognized by Monoclonal Antibodies against HP-PRRSV: Deep Understanding of Antigenic Structure and Virus-Antibody Interaction |
title_full_unstemmed | Unique Epitopes Recognized by Monoclonal Antibodies against HP-PRRSV: Deep Understanding of Antigenic Structure and Virus-Antibody Interaction |
title_short | Unique Epitopes Recognized by Monoclonal Antibodies against HP-PRRSV: Deep Understanding of Antigenic Structure and Virus-Antibody Interaction |
title_sort | unique epitopes recognized by monoclonal antibodies against hp-prrsv: deep understanding of antigenic structure and virus-antibody interaction |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4216098/ https://www.ncbi.nlm.nih.gov/pubmed/25360600 http://dx.doi.org/10.1371/journal.pone.0111633 |
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