{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T04:49:32Z","timestamp":1791521372829,"version":"4.3.4"},"reference-count":43,"publisher":"National Academy of Sciences","issue":"31","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2009,8,4]]},"abstract":"<jats:p>\n                    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-\u212b resolution. The capsid protein exhibited a quite different folding at the protruding and middle domains from the members of the families of\n                    <jats:italic>Caliciviridae<\/jats:italic>\n                    and\n                    <jats:italic>Tombusviridae<\/jats:italic>\n                    , 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.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0903699106","type":"journal-article","created":{"date-parts":[[2009,7,21]],"date-time":"2009-07-21T21:07:45Z","timestamp":1248210465000},"page":"12986-12991","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":247,"title":["Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure"],"prefix":"10.1073","volume":"106","author":[{"given":"Tetsuo","family":"Yamashita","sequence":"first","affiliation":[{"name":"Department of Molecular Virology, Research Institute for Microbial Diseases and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshio","family":"Mori","sequence":"additional","affiliation":[{"name":"Department of Molecular Virology, Research Institute for Microbial Diseases and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naoyuki","family":"Miyazaki","sequence":"additional","affiliation":[{"name":"Department of Protein Crystallography, Research Institute for Protein Research, Osaka University, Osaka 565-0871, Japan;"},{"name":"Department of Molecular and Cellular Biology, University of California, Davis, CA 95616;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R. 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