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

Research output: Contribution to journalArticle

149 Citations (Scopus)

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

Fingerprint

Hepatitis E virus
Virion
Capsid Proteins
Tombusviridae
Caliciviridae
Hepatitis E
Aromatic Amino Acids
Virus Diseases
Hepatitis
Epitopes
Viruses

Keywords

  • Capsid
  • HEV
  • VLP

ASJC Scopus subject areas

  • General

Cite this

Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure. / Yamashita, Tetsuo; Mori, Yoshio; Miyazaki, Naoyuki; Cheng, R. Holland; Yoshimura, Masato; Unno, Hideaki; Shima, Ryoichi; Moriishi, Kohji; Tsukihara, Tomitake; Tian, Cheng Li; Takeda, Naokazu; Miyamura, Tatsuo; Matsuura, Yoshiharu.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 106, No. 31, 04.08.2009, p. 12986-12991.

Research output: Contribution to journalArticle

Yamashita, T, Mori, Y, Miyazaki, N, Cheng, RH, Yoshimura, M, Unno, H, Shima, R, Moriishi, K, Tsukihara, T, Tian, CL, 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, vol. 106, no. 31, pp. 12986-12991. https://doi.org/10.1073/pnas.0903699106
Yamashita, Tetsuo ; Mori, Yoshio ; Miyazaki, Naoyuki ; Cheng, R. Holland ; Yoshimura, Masato ; Unno, Hideaki ; Shima, Ryoichi ; Moriishi, Kohji ; Tsukihara, Tomitake ; Tian, Cheng Li ; Takeda, Naokazu ; Miyamura, Tatsuo ; Matsuura, Yoshiharu. / Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure. In: Proceedings of the National Academy of Sciences of the United States of America. 2009 ; Vol. 106, No. 31. pp. 12986-12991.
@article{ce3f7d14c9bb4ce586e707148727b78b,
title = "Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure",
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-{\AA} 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.",
keywords = "Capsid, HEV, VLP",
author = "Tetsuo Yamashita and Yoshio Mori and Naoyuki Miyazaki and Cheng, {R. Holland} and Masato Yoshimura and Hideaki Unno and Ryoichi Shima and Kohji Moriishi and Tomitake Tsukihara and Tian, {Cheng Li} and Naokazu Takeda and Tatsuo Miyamura and Yoshiharu Matsuura",
year = "2009",
month = "8",
day = "4",
doi = "10.1073/pnas.0903699106",
language = "English (US)",
volume = "106",
pages = "12986--12991",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "31",

}

TY - JOUR

T1 - Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure

AU - Yamashita, Tetsuo

AU - Mori, Yoshio

AU - Miyazaki, Naoyuki

AU - Cheng, R. Holland

AU - Yoshimura, Masato

AU - Unno, Hideaki

AU - Shima, Ryoichi

AU - Moriishi, Kohji

AU - Tsukihara, Tomitake

AU - Tian, Cheng Li

AU - Takeda, Naokazu

AU - Miyamura, Tatsuo

AU - Matsuura, Yoshiharu

PY - 2009/8/4

Y1 - 2009/8/4

N2 - 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.

AB - 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.

KW - Capsid

KW - HEV

KW - VLP

UR - http://www.scopus.com/inward/record.url?scp=69149100932&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=69149100932&partnerID=8YFLogxK

U2 - 10.1073/pnas.0903699106

DO - 10.1073/pnas.0903699106

M3 - Article

C2 - 19620712

AN - SCOPUS:69149100932

VL - 106

SP - 12986

EP - 12991

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 31

ER -