Identification of a conserved B-cell epitope on duck hepatitis A type 1 virus VP1 protein.
<h4>Background</h4>The VP1 protein of duck hepatitis A virus (DHAV) is a major structural protein that induces neutralizing antibodies in ducks; however, B-cell epitopes on the VP1 protein of duck hepatitis A genotype 1 virus (DHAV-1) have not been characterized.<h4>Methods and res...
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Public Library of Science (PLoS)
2015-01-01
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| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0118041&type=printable |
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| author | Xiaoying Wu Xiaojun Li Qingshan Zhang Shaozhou Wulin Xiaofei Bai Tingting Zhang Yue Wang Ming Liu Yun Zhang |
| author_facet | Xiaoying Wu Xiaojun Li Qingshan Zhang Shaozhou Wulin Xiaofei Bai Tingting Zhang Yue Wang Ming Liu Yun Zhang |
| author_sort | Xiaoying Wu |
| collection | DOAJ |
| description | <h4>Background</h4>The VP1 protein of duck hepatitis A virus (DHAV) is a major structural protein that induces neutralizing antibodies in ducks; however, B-cell epitopes on the VP1 protein of duck hepatitis A genotype 1 virus (DHAV-1) have not been characterized.<h4>Methods and results</h4>To characterize B-cell epitopes on VP1, we used the monoclonal antibody (mAb) 2D10 against Escherichia coli-expressed VP1 of DHAV-1. In vitro, mAb 2D10 neutralized DHAV-1 virus. By using an array of overlapping 12-mer peptides, we found that mAb 2D10 recognized phages displaying peptides with the consensus motif LPAPTS. Sequence alignment showed that the epitope 173LPAPTS178 is highly conserved among the DHAV-1 genotypes. Moreover, the six amino acid peptide LPAPTS was proven to be the minimal unit of the epitope with maximal binding activity to mAb 2D10. DHAV-1-positive duck serum reacted with the epitope in dot blotting assay, revealing the importance of the six amino acids of the epitope for antibody-epitope binding. Competitive inhibition assays of mAb 2D10 binding to synthetic LPAPTS peptides and truncated VP1 protein fragments, detected by Western blotting, also verify that LPAPTS was the VP1 epitope.<h4>Conclusions and significance</h4>We identified LPAPTS as a VP1-specific linear B-cell epitope recognized by the neutralizing mAb 2D10. Our findings have potential applications in the development of diagnostic techniques and epitope-based marker vaccines against DHAV-1. |
| format | Article |
| id | doaj-art-44dfad9f397b40c5b4a465d8166089ff |
| institution | DOAJ |
| issn | 1932-6203 |
| language | English |
| publishDate | 2015-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-44dfad9f397b40c5b4a465d8166089ff2025-08-20T03:01:29ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01102e011804110.1371/journal.pone.0118041Identification of a conserved B-cell epitope on duck hepatitis A type 1 virus VP1 protein.Xiaoying WuXiaojun LiQingshan ZhangShaozhou WulinXiaofei BaiTingting ZhangYue WangMing LiuYun Zhang<h4>Background</h4>The VP1 protein of duck hepatitis A virus (DHAV) is a major structural protein that induces neutralizing antibodies in ducks; however, B-cell epitopes on the VP1 protein of duck hepatitis A genotype 1 virus (DHAV-1) have not been characterized.<h4>Methods and results</h4>To characterize B-cell epitopes on VP1, we used the monoclonal antibody (mAb) 2D10 against Escherichia coli-expressed VP1 of DHAV-1. In vitro, mAb 2D10 neutralized DHAV-1 virus. By using an array of overlapping 12-mer peptides, we found that mAb 2D10 recognized phages displaying peptides with the consensus motif LPAPTS. Sequence alignment showed that the epitope 173LPAPTS178 is highly conserved among the DHAV-1 genotypes. Moreover, the six amino acid peptide LPAPTS was proven to be the minimal unit of the epitope with maximal binding activity to mAb 2D10. DHAV-1-positive duck serum reacted with the epitope in dot blotting assay, revealing the importance of the six amino acids of the epitope for antibody-epitope binding. Competitive inhibition assays of mAb 2D10 binding to synthetic LPAPTS peptides and truncated VP1 protein fragments, detected by Western blotting, also verify that LPAPTS was the VP1 epitope.<h4>Conclusions and significance</h4>We identified LPAPTS as a VP1-specific linear B-cell epitope recognized by the neutralizing mAb 2D10. Our findings have potential applications in the development of diagnostic techniques and epitope-based marker vaccines against DHAV-1.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0118041&type=printable |
| spellingShingle | Xiaoying Wu Xiaojun Li Qingshan Zhang Shaozhou Wulin Xiaofei Bai Tingting Zhang Yue Wang Ming Liu Yun Zhang Identification of a conserved B-cell epitope on duck hepatitis A type 1 virus VP1 protein. PLoS ONE |
| title | Identification of a conserved B-cell epitope on duck hepatitis A type 1 virus VP1 protein. |
| title_full | Identification of a conserved B-cell epitope on duck hepatitis A type 1 virus VP1 protein. |
| title_fullStr | Identification of a conserved B-cell epitope on duck hepatitis A type 1 virus VP1 protein. |
| title_full_unstemmed | Identification of a conserved B-cell epitope on duck hepatitis A type 1 virus VP1 protein. |
| title_short | Identification of a conserved B-cell epitope on duck hepatitis A type 1 virus VP1 protein. |
| title_sort | identification of a conserved b cell epitope on duck hepatitis a type 1 virus vp1 protein |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0118041&type=printable |
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