Characterization of antigenic domains and epitopes in the ORF3 protein of a Chinese isolate of avian hepatitis E virus

2013 ◽  
Vol 167 (3-4) ◽  
pp. 242-249 ◽  
Author(s):  
Qin Zhao ◽  
Ya-ni Sun ◽  
Shou-bin Hu ◽  
Xin-jie Wang ◽  
Yi-hong Xiao ◽  
...  
Virus Genes ◽  
2016 ◽  
Vol 52 (5) ◽  
pp. 738-742 ◽  
Author(s):  
Hyun-Woo Moon ◽  
Byung-Woo Lee ◽  
Haan Woo Sung ◽  
Byung-Il Yoon ◽  
Hyuk Moo Kwon

2019 ◽  
Vol 11 (2) ◽  
pp. 45-50
Author(s):  
B. Ouoba Jean ◽  
A. Traore Kuan ◽  
K. M’Bengue Alphonsine ◽  
Ngazoa Solange ◽  
Rouamba Hortense ◽  
...  

2014 ◽  
Vol 95 (12) ◽  
pp. 2710-2715 ◽  
Author(s):  
Lizhen Wang ◽  
Yani Sun ◽  
Taofeng Du ◽  
Chengbao Wang ◽  
Shuqi Xiao ◽  
...  

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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