Dimerization of hepatitis E virus capsid protein E2s domain is essential for virus-host interaction

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 b...

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Bibliographic Details
Published in:PLoS pathogens 2009-08, Vol.5 (8), p.e1000537-e1000537
Main Authors: Li, Shaowei, Tang, Xuhua, Seetharaman, J, Yang, Chunyan, Gu, Ying, Zhang, Jun, Du, Hailian, Shih, J Wai Kuo, Hew, Choy-Leong, Sivaraman, J, Xia, Ningshao
Format: Article
Language:English
Subjects:
antibodies
Antigens, Viral - chemistry
Antigens, Viral - genetics
Antigens, Viral - immunology
Base Sequence
BASIC BIOLOGICAL SCIENCES
Blotting, Western
Capsid Proteins - chemistry
Capsid Proteins - genetics
Capsid Proteins - immunology
crystal structure
Development and progression
dimerization
dimers
Disease
Electrophoresis, Polyacrylamide Gel
Genetic aspects
Hepatitis E
hepatitis E virus
Hepatitis E virus - chemistry
Hepatitis E virus - genetics
Hepatitis E virus - immunology
Host-Parasite Interactions - physiology
Host-virus relationships
Industrialized nations
Molecular Sequence Data
Molecular weight
Mortality
Mutation
Physiological aspects
point mutation
protein domains
Protein Multimerization
Protein Structure, Quaternary
Proteins
Vaccines
Viral infections
viral packaging
Viral proteins
Virology/Vaccines
Virology/Virion Structure, Assembly, and Egress
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Summary: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.
ISSN:1553-7374
1553-7366
1553-7374
DOI:10.1371/journal.ppat.1000537