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Identification of an antigenic domain in the N-terminal region of avian hepatitis E virus (HEV) capsid protein that is not common to swine and human HEVs
Author(s) -
Lizhen Wang,
Yani Sun,
Taofeng Du,
Chengbao Wang,
Shuqi Xiao,
Yang Mu,
Gaiping Zhang,
Lihong Liu,
Frederik Widén,
Walter H. Hsu,
Qin Zhao,
EnMin Zhou
Publication year - 2014
Publication title -
journal of general virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.55
H-Index - 167
eISSN - 1465-2099
pISSN - 0022-1317
DOI - 10.1099/vir.0.069021-0
Subject(s) - capsid , virology , epitope , hepatitis e virus , antigenicity , biology , recombinant dna , antigen , epitope mapping , amino acid , virus , genetics , gene , genotype
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.

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