Dimerization of Hepatitis E Virus Capsid Protein E2s Domain Is Essential for Virus–Host Interaction

PLoS Pathogens

Chunyan Yang¹  Jun Zhang²  Ningshao Xia²  Shaowei Li²  J. Sivaraman²  J. Wai Kuo Shih²  Hailian Du²  Ying Gu³  Choy-Leong Hew⁴  J. Seetharaman⁴  Xuhua Tang⁴ 

[1] Department of Biological Sciences, National University of Singapore, Singapore;National Institute of Diagnostics and Vaccine Development in Infectious Disease, School of Life Sciences, Xiamen University, Xiamen, China;X4 Beamline, Brookhaven National Laboratory, Upton, New York, United States of America;Xiamen-NUS Joint Laboratory in Biomedical Sciences, Xiamen University, Xiamen, China

关键词: Hepatitis E virus;    Dimers (Chemical physics);    Dimerization;    Viral packaging;    Crystal structure;    Antibodies;    Protein domains;    Point mutation;   

DOI  :  10.1371/journal.ppat.1000537

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

Hepatitis E virus (HEV), a non-enveloped, positive-stranded RNA virus, is transmitted in a faecal-oral manner, and causes acute liver diseases in humans. The HEV capsid is made up of capsomeres consisting of homodimers of a single structural capsid protein forming the virus shell. These dimers are believed to protrude from the viral surface and to interact with host cells to initiate infection. To date, no structural information is available for any of the HEV proteins. Here, we report for the first time the crystal structure of the HEV capsid protein domain E2s, a protruding domain, together with functional studies to illustrate that this domain forms a tight homodimer and that this dimerization is essential for HEV–host interactions. In addition, we also show that the neutralizing antibody recognition site of HEV is located on the E2s domain. Our study will aid in the development of vaccines and, subsequently, specific inhibitors for HEV.

【 授权许可】

CC BY