Identification of a conserved B-cell epitope on duck hepatitis A type 1 virus VP1 protein.

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.To characterize B-cell epitopes on VP1, we used the mono...

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Main Authors: Xiaoying Wu, Xiaojun Li, Qingshan Zhang, Shaozhou Wulin, Xiaofei Bai, Tingting Zhang, Yue Wang, Ming Liu, Yun Zhang
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4337900?pdf=render
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spelling doaj-44dfad9f397b40c5b4a465d8166089ff2020-11-24T21:50:43ZengPublic 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 ZhangThe 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.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.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.http://europepmc.org/articles/PMC4337900?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Xiaoying Wu
Xiaojun Li
Qingshan Zhang
Shaozhou Wulin
Xiaofei Bai
Tingting Zhang
Yue Wang
Ming Liu
Yun Zhang
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
author_facet Xiaoying Wu
Xiaojun Li
Qingshan Zhang
Shaozhou Wulin
Xiaofei Bai
Tingting Zhang
Yue Wang
Ming Liu
Yun Zhang
author_sort Xiaoying Wu
title 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_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_sort identification of a conserved b-cell epitope on duck hepatitis a type 1 virus vp1 protein.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2015-01-01
description 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.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.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.
url http://europepmc.org/articles/PMC4337900?pdf=render
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