Role of the C-terminal cysteines in virus-like particle formation and oligomerization of the hepatitis E virus ORF2 truncated proteins

被引：7
|
作者：
Liu, Zhenzhen [1 ,2 ]
Behloul, Nouredine [1 ]
Baha, Sarra [2 ]
Wei, Wenjuan [2 ]
Tao, Wanru [3 ]
Zhang, Tingying [1 ]
Li, Wei [1 ,3 ]
Shi, Ruihua [2 ]
Meng, Jihong [1 ,2 ]
机构：
[1] Shanghai Univ Med & Hlth Sci, Coll Basic Med, Shanghai 201318, Peoples R China
[2] Southeast Univ, Zhongda Hosp, Dept Gastroenterol, Nanjing 210009, Jiangsu, Peoples R China
[3] Second Mil Med Univ, Lab Nano Biomed, Shanghai 200433, Peoples R China
来源：
VIROLOGY | 2020年 / 544卷
基金：
中国国家自然科学基金;
关键词：
Hepatitis E virus; Virus-like particle; Capsid assembly; Disulfide bond; CAPSID PROTEIN; DISULFIDE BONDS; IMMUNOMAGNETIC SEPARATION; STRUCTURAL BASIS; NON-A; NEUTRALIZATION; DIMERIZATION; PREDICTION;
D O I：
10.1016/j.virol.2020.01.011
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
The hepatitis E virus (HEV) ORF2 truncated recombinant proteins can self-assemble into virus-like particles (VLPs) and were used as models to investigate the HEV capsid assembly. However, the structural function of the ORF2 C-terminal domain (C52aa from aa 608 to aa 660) remains unclear. Herein, by analyzing a set of ORF2 truncated proteins expressed in Escherichia coli, we found that the highly conserved C-terminal cysteines play a crucial role in the oligomerization of the truncated ORF2 proteins and in their assembly into VLPs, through the formation of dimer-dimer disulfide bonds; and the treatment of native HEV particles with dithiothreitol (DTT) induced the disassembly of the viral capsid, suggesting that the disulfide bonding is required for stabilizing the native HEV capsid. The present study sheds light on the structural role of the C-terminal region of the HEV capsid protein and contributes to the full understating of the viral capsid assembly process.
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页码：1 / 11
页数：11
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