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

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

doi:10.1371/journal.ppat.1000537

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

Journal Article · 06 August 2009 · PLoS Pathogens

DOI: https://doi.org/10.1371/journal.ppat.1000537 · OSTI ID:1627893

Li, Shaowei ^[1]; Tang, Xuhua ^[2]; Seetharaman, J. ^[3]; Yang, Chunyan ^[4]; Gu, Ying ^[4]; Zhang, Jun ^[4]; Du, Hailian ^[4]; Shih, J. Wai Kuo ^[4]; Hew, Choy-Leong ^[4]; Sivaraman, J. ^[2]; Xia, Ningshao ^[4]

Xiamen University (China); DOE/OSTI
Xiamen University (China); National University of Singapore (Singapore)
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Xiamen University (China)

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.

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: Academic Research Fund; Key Program in Infectious Diseases; Ministry of Education; National Natural Science Foundation; National University of Singapore; People's Republic of China; USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: SC0012704

OSTI ID:: 1627893

Journal Information:: PLoS Pathogens, Journal Name: PLoS Pathogens Journal Issue: 8 Vol. 5; ISSN 1553-7374

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
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Title: Dimerization of Hepatitis E Virus Capsid Protein E2s Domain Is Essential for Virus–Host Interaction

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