| Literature DB >> 25209807 |
Lizhen Wang1,2, Yani Sun1,2, Taofeng Du1,2, Chengbao Wang1,2, Shuqi Xiao1,2, Yang Mu1,2, Gaiping Zhang3,2, Lihong Liu4, Frederik Widén4, Walter H Hsu5, Qin Zhao1,2, En-Min Zhou1,2.
Abstract
The antigenic domains located in the C-terminal 268 amino acid residues of avian hepatitis E virus (HEV) capsid protein have been characterized. This region shares common epitopes with swine and human HEVs. However, epitopes in the N-terminal 338 amino acid residues have never been reported. In this study, an antigenic domain located between amino acids 23 and 85 was identified by indirect ELISA using the truncated recombinant capsid proteins as coating antigens and anti-avian HEV chicken sera as primary antibodies. In addition, this domain did not react with anti-swine and human HEV sera. These results indicated that the N-terminal 338 amino acid residues of avian HEV capsid protein do not share common epitopes with swine and human HEVs. This finding is important for our understanding of the antigenicity of the avian HEV capsid protein. Furthermore, it has important implications in the selection of viral antigens for serological diagnosis.Entities:
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Year: 2014 PMID： 25209807 DOI： 10.1099/vir.0.069021-0
Source DB: PubMed Journal: J Gen Virol ISSN： 0022-1317 Impact factor: 3.891