Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.ppat.1000537
Title: Dimerization of hepatitis E virus capsid protein E2s domain is essential for virus-host interaction
Authors: Li, S.
Tang, X. 
Seetharaman, J.
Yang, C.
Gu, Y.
Zhang, J.
Du, H.
Shih, J.W.K.
Hew, C.-L. 
Sivaraman, J. 
Xia, N.
Issue Date: Aug-2009
Citation: Li, S., Tang, X., Seetharaman, J., Yang, C., Gu, Y., Zhang, J., Du, H., Shih, J.W.K., Hew, C.-L., Sivaraman, J., Xia, N. (2009-08). Dimerization of hepatitis E virus capsid protein E2s domain is essential for virus-host interaction. PLoS Pathogens 5 (8) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.ppat.1000537
Abstract: 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. © 2009 Li et al.
Source Title: PLoS Pathogens
URI: http://scholarbank.nus.edu.sg/handle/10635/100467
ISSN: 15537366
DOI: 10.1371/journal.ppat.1000537
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