Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure

Tetsuo Yamashita, Yoshio Mori, Naoyuki Miyazaki, R. Holland Cheng, Masato Yoshimura, Hideaki Unno, Ryoichi Shima, Kohji Moriishi, Tomitake Tsukihara, Cheng Li Tian, Naokazu Takeda, Tatsuo Miyamura, Yoshiharu Matsuura

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Abstract

Hepatitis E virus (HEV) is a causative agent of acute hepatitis. The crystal structure of HEV-like particles (HEV-LP) consisting of capsid protein was determined at 3.5-Å resolution. The capsid protein exhibited a quite different folding at the protruding and middle domains from the members of the families of Caliciviridae and Tombusviridae, while the shell domain shared the common folding. Tyr-288 at the 5-fold axis plays key roles in the assembly of HEV-LP, and aromatic amino acid residues are well conserved among the structurally related viruses. Mutational analyses indicated that the protruding domain is involved in the binding to the cells susceptive to HEV infection and has some neutralization epitopes. These structural and biological findings are important for understanding the molecular mechanisms of assembly and entry of HEV and also provide clues in the development of preventive and prophylactic measures for hepatitis E.

Original languageEnglish (US)
Pages (from-to)12986-12991
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume106
Issue number31
DOIs
StatePublished - Aug 4 2009

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Keywords

  • Capsid
  • HEV
  • VLP

ASJC Scopus subject areas

  • General

Cite this

Yamashita, T., Mori, Y., Miyazaki, N., Cheng, R. H., Yoshimura, M., Unno, H., Shima, R., Moriishi, K., Tsukihara, T., Tian, C. L., Takeda, N., Miyamura, T., & Matsuura, Y. (2009). Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure. Proceedings of the National Academy of Sciences of the United States of America, 106(31), 12986-12991. https://doi.org/10.1073/pnas.0903699106