| Literature DB >> 19620712 |
Tetsuo Yamashita1, Yoshio Mori, Naoyuki Miyazaki, R Holland Cheng, Masato Yoshimura, Hideaki Unno, Ryoichi Shima, Kohji Moriishi, Tomitake Tsukihara, Tian Cheng Li, Naokazu Takeda, Tatsuo Miyamura, Yoshiharu Matsuura.
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-A 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.Entities:
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Year: 2009 PMID： 19620712 PMCID： PMC2722322 DOI： 10.1073/pnas.0903699106
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205