Structure of hepatitis E viral particle

Hepatitis E is acute hepatitis caused by infection of hepatitis E virus (HEV) via a fecal-to-oral or zoonotic route. HEV is a small, non-enveloped virus containing positive strand RNA as a genome. Recently, the three-dimensional structures of the HEV-like particles and spike domain protruded from th...

Full description

Saved in:
Bibliographic Details
Published inVirus research Vol. 161; no. 1; pp. 59 - 64
Main Authors Mori, Yoshio, Matsuura, Yoshiharu
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.10.2011
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Hepatitis E is acute hepatitis caused by infection of hepatitis E virus (HEV) via a fecal-to-oral or zoonotic route. HEV is a small, non-enveloped virus containing positive strand RNA as a genome. Recently, the three-dimensional structures of the HEV-like particles and spike domain protruded from the surface of the particle expressed by recombinant baculovirus or bacteria have been revealed. Based on these reports, the structural features of the HEV capsid subunit and viral particle are reviewed to give insights to the mechanisms underlying the particle assembly, antigenicity, host cell attachment and native virion packaging.
AbstractList Hepatitis E is acute hepatitis caused by infection of hepatitis E virus (HEV) via a fecal-to-oral or zoonotic route. HEV is a small, non-enveloped virus containing positive strand RNA as a genome. Recently, the three-dimensional structures of the HEV-like particles and spike domain protruded from the surface of the particle expressed by recombinant baculovirus or bacteria have been revealed. Based on these reports, the structural features of the HEV capsid subunit and viral particle are reviewed to give insights to the mechanisms underlying the particle assembly, antigenicity, host cell attachment and native virion packaging.
Hepatitis E is acute hepatitis caused by infection of hepatitis E virus (HEV) via a fecal-to-oral or zoonotic route. HEV is a small, non-enveloped virus containing positive strand RNA as a genome. Recently, the three-dimensional structures of the HEV-like particles and spike domain protruded from the surface of the particle expressed by recombinant baculovirus or bacteria have been revealed. Based on these reports, the structural features of the HEV capsid subunit and viral particle are reviewed to give insights to the mechanisms underlying the particle assembly, antigenicity, host cell attachment and native virion packaging.Hepatitis E is acute hepatitis caused by infection of hepatitis E virus (HEV) via a fecal-to-oral or zoonotic route. HEV is a small, non-enveloped virus containing positive strand RNA as a genome. Recently, the three-dimensional structures of the HEV-like particles and spike domain protruded from the surface of the particle expressed by recombinant baculovirus or bacteria have been revealed. Based on these reports, the structural features of the HEV capsid subunit and viral particle are reviewed to give insights to the mechanisms underlying the particle assembly, antigenicity, host cell attachment and native virion packaging.
Author Mori, Yoshio
Matsuura, Yoshiharu
Author_xml – sequence: 1
  givenname: Yoshio
  surname: Mori
  fullname: Mori, Yoshio
  organization: Department of Molecular Virology, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamada-oka, Suita, Osaka 565-0871, Japan
– sequence: 2
  givenname: Yoshiharu
  surname: Matsuura
  fullname: Matsuura, Yoshiharu
  email: matsuura@biken.osaka-u.ac.jp
  organization: Department of Molecular Virology, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamada-oka, Suita, Osaka 565-0871, Japan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/21440590$$D View this record in MEDLINE/PubMed
BookMark eNqFkU9rGzEQxUVJaBy3X8HdW3rZzejPalfQQ4Nxk4ChhzRnIcujRma960paQ799ZRz3kEMsGATD7400712Ti37okZAZhYoClbebau_DGAPGigGlFfAKaP2BTGjbsLIRil2QSQbbkjbArsh1jBsAkLyRH8kVo0JArWBCbp5SGG0aAxaDK15wZ5JPPhaLIs83XbEzIXnb4Sdy6UwX8fPrPSXPPxa_5g_l8uf94_xuWdqasVQKrjhyDhIMmlo4ZA01ggojlbRr6hrRCqkcIDoOq9zLtZKmteiYhBXjU3JznLsLw58RY9JbHy12nelxGKNWwPIKgtVnyVZx1Sqhmkx-fZdkcDgNKJXR2Ss6rra41rvgtyb81SfDMiCPgA1DzPa7_wgFfUhGb_QpGX1IRgPXOZks_PZGaH3KZg99CsZ35-VfjnJnBm1-Bx_181MGZP45q2s4bPn9SGCOZ-8x6Gg99hbXPqBNej34c4_8A_EgtVw
CitedBy_id crossref_primary_10_3389_fmicb_2020_00141
crossref_primary_10_1016_j_jhepr_2024_101293
crossref_primary_10_1016_j_vaccine_2015_12_068
crossref_primary_10_1016_j_csbj_2021_03_038
crossref_primary_10_1099_jgv_0_001778
crossref_primary_10_3390_v11060539
crossref_primary_10_1016_j_vaccine_2015_05_065
crossref_primary_10_3389_fmicb_2016_01419
crossref_primary_10_1007_s42485_021_00075_w
crossref_primary_10_1016_j_virusres_2018_03_018
crossref_primary_10_3390_v15071558
crossref_primary_10_1111_tid_12699
crossref_primary_10_1016_j_abb_2012_10_015
crossref_primary_10_58395_y45wev44
crossref_primary_10_4142_jvs_2014_15_4_575
crossref_primary_10_3389_fmicb_2017_02396
crossref_primary_10_1038_srep25735
crossref_primary_10_1039_C7AY00048K
crossref_primary_10_1016_j_virol_2020_01_011
crossref_primary_10_1038_nrgastro_2012_187
crossref_primary_10_1099_vir_0_051870_0
crossref_primary_10_4049_jimmunol_2300706
crossref_primary_10_1007_s00705_022_05575_8
crossref_primary_10_1016_j_vaccine_2013_11_064
crossref_primary_10_1080_17474124_2016_1185362
crossref_primary_10_3389_fmicb_2019_02481
crossref_primary_10_1099_vir_0_049577_0
crossref_primary_10_2217_fvl_15_17
crossref_primary_10_3390_cells9051294
crossref_primary_10_1007_s00103_022_03487_1
crossref_primary_10_1128_JVI_00251_18
crossref_primary_10_1111_j_1365_2893_2011_01559_x
crossref_primary_10_1128_JVI_00444_13
crossref_primary_10_1186_s43141_021_00238_8
crossref_primary_10_1016_j_meegid_2018_07_029
crossref_primary_10_1099_jgv_0_000940
crossref_primary_10_3390_pathogens10091206
crossref_primary_10_1007_s00535_012_0682_0
crossref_primary_10_3390_v12010109
crossref_primary_10_1016_j_coviro_2015_04_003
crossref_primary_10_1016_j_jhep_2022_08_002
crossref_primary_10_3389_fmicb_2018_00266
crossref_primary_10_1186_s43088_022_00244_w
crossref_primary_10_1016_j_meegid_2014_01_002
crossref_primary_10_1186_s43141_022_00319_2
crossref_primary_10_1002_jmv_24567
crossref_primary_10_1016_j_jviromet_2013_03_010
crossref_primary_10_2174_2772270817666230112123221
crossref_primary_10_1038_s41598_018_20137_2
crossref_primary_10_1016_j_jviromet_2011_05_001
crossref_primary_10_3389_fmicb_2021_739124
crossref_primary_10_3390_v13071329
crossref_primary_10_1016_S1665_2681_19_31250_5
crossref_primary_10_1159_000515719
crossref_primary_10_1016_j_jhep_2016_02_045
crossref_primary_10_1099_vir_0_059238_0
crossref_primary_10_1016_j_meegid_2015_11_006
crossref_primary_10_3748_wjg_v27_i20_2458
crossref_primary_10_1007_s00253_017_8622_9
Cites_doi 10.1016/S0140-6736(10)61030-6
10.1073/pnas.0803275105
10.1128/JVI.74.12.5548-5555.2000
10.1099/vir.0.81545-0
10.1099/vir.0.016584-0
10.1016/j.virol.2006.02.038
10.1128/JVI.00717-09
10.1159/000149370
10.1128/JVI.01976-07
10.1099/vir.0.83308-0
10.1128/JVI.70.1.207-216.1996
10.1099/0022-1317-65-5-1005
10.1371/journal.ppat.1000537
10.1128/JVI.00135-08
10.1073/pnas.0904848106
10.1016/j.virusres.2007.02.002
10.1006/viro.1999.0005
10.1007/s00705-008-0045-6
10.1074/jbc.M110.106336
10.1073/pnas.0600421103
10.1016/j.vaccine.2003.08.004
10.1128/JVI.79.20.12999-13006.2005
10.1128/JVI.71.10.7207-7213.1997
10.1002/rmv.522
10.1006/viro.2001.1240
10.1099/0022-1317-69-3-731
10.1128/JVI.00550-08
10.1016/j.vaccine.2003.07.008
10.1099/vir.0.010561-0
10.1073/pnas.0903699106
10.1128/JVI.00807-07
10.1007/s00705-008-0179-6
10.1056/NEJMoa061847
10.1126/science.286.5438.287
10.1038/sj.gt.3302193
ContentType Journal Article
Copyright 2011 Elsevier B.V.
Copyright © 2011 Elsevier B.V. All rights reserved.
Copyright_xml – notice: 2011 Elsevier B.V.
– notice: Copyright © 2011 Elsevier B.V. All rights reserved.
DBID FBQ
AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7S9
L.6
7X8
7U9
H94
DOI 10.1016/j.virusres.2011.03.015
DatabaseName AGRIS
CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
AGRICOLA
AGRICOLA - Academic
MEDLINE - Academic
Virology and AIDS Abstracts
AIDS and Cancer Research Abstracts
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
AGRICOLA
AGRICOLA - Academic
MEDLINE - Academic
AIDS and Cancer Research Abstracts
Virology and AIDS Abstracts
DatabaseTitleList
AGRICOLA
MEDLINE
AIDS and Cancer Research Abstracts

MEDLINE - Academic
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 3
  dbid: FBQ
  name: AGRIS
  url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN
  sourceTypes: Publisher
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 1872-7492
EndPage 64
ExternalDocumentID 21440590
10_1016_j_virusres_2011_03_015
US201600025507
S0168170211001055
Genre Research Support, Non-U.S. Gov't
Journal Article
Review
GroupedDBID ---
--K
--M
.GJ
.~1
0R~
0SF
123
1B1
1RT
1~.
1~5
29Q
4.4
457
4G.
53G
5RE
5VS
7-5
71M
8P~
9JM
AAAJQ
AABNK
AACTN
AAEDT
AAEDW
AAIAV
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AAQXK
AARKO
AAXUO
ABBQC
ABFNM
ABFRF
ABJNI
ABLVK
ABMAC
ABMZM
ABXDB
ABYKQ
ACDAQ
ACGFO
ACGFS
ACIUM
ACRLP
ADBBV
ADEZE
ADMUD
AEBSH
AEFWE
AEKER
AENEX
AFKWA
AFTJW
AFXIZ
AGEKW
AGHFR
AGUBO
AGYEJ
AHHHB
AIEXJ
AIKHN
AITUG
AJBFU
AJOXV
AJRQY
ALMA_UNASSIGNED_HOLDINGS
AMFUW
AMRAJ
ANZVX
ASPBG
AVWKF
AXJTR
AZFZN
BKOJK
BLXMC
BNPGV
CJTIS
CNWQP
CS3
DU5
EBS
EFJIC
EFLBG
EJD
EO8
EO9
EP2
EP3
F5P
FDB
FEDTE
FGOYB
FIRID
FNPLU
FYGXN
G-2
G-Q
GBLVA
GROUPED_DOAJ
HMG
HVGLF
HZ~
IH2
IHE
J1W
KOM
LCYCR
LUGTX
M41
MO0
N9A
O-L
O9-
OAUVE
OZT
P-8
P-9
P2P
PC.
Q38
R2-
RIG
ROL
RPM
RPZ
SCC
SDF
SDG
SDP
SES
SEW
SIN
SPCBC
SSH
SSI
SSZ
T5K
WH7
WUQ
ZGI
~G-
ABPIF
ABPTK
FBQ
AAHBH
AATTM
AAXKI
AAYWO
AAYXX
ABWVN
ACIEU
ACRPL
ACVFH
ADCNI
ADNMO
ADVLN
AEIPS
AEUPX
AFJKZ
AFPUW
AGCQF
AGQPQ
AGRNS
AIGII
AIIUN
AKBMS
AKRWK
AKYEP
ANKPU
APXCP
CITATION
CGR
CUY
CVF
ECM
EFKBS
EIF
NPM
7S9
L.6
7X8
7U9
H94
ID FETCH-LOGICAL-c522t-4393e33060aea54fe271a414a696cd1f748469f0eef30b96cb96b6a8cef260b23
IEDL.DBID .~1
ISSN 0168-1702
1872-7492
IngestDate Sun Aug 24 03:21:54 EDT 2025
Fri Jul 11 15:59:16 EDT 2025
Fri Jul 11 06:42:14 EDT 2025
Mon Jul 21 06:00:59 EDT 2025
Thu Apr 24 23:06:52 EDT 2025
Tue Jul 01 01:45:06 EDT 2025
Wed Dec 27 19:09:43 EST 2023
Fri Feb 23 02:28:24 EST 2024
IsPeerReviewed true
IsScholarly true
Issue 1
Keywords NOB
Particle assembly
ORF
Capsid protein
HEV
HEV-LP
HSPGs
Hepatitis E virus
Crystal structure
Language English
License https://www.elsevier.com/tdm/userlicense/1.0
Copyright © 2011 Elsevier B.V. All rights reserved.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c522t-4393e33060aea54fe271a414a696cd1f748469f0eef30b96cb96b6a8cef260b23
Notes http://dx.doi.org/10.1016/j.virusres.2011.03.015
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ObjectType-Review-3
ObjectType-Article-2
ObjectType-Feature-1
PMID 21440590
PQID 2000007099
PQPubID 24069
PageCount 6
ParticipantIDs proquest_miscellaneous_902376425
proquest_miscellaneous_893989497
proquest_miscellaneous_2000007099
pubmed_primary_21440590
crossref_primary_10_1016_j_virusres_2011_03_015
crossref_citationtrail_10_1016_j_virusres_2011_03_015
fao_agris_US201600025507
elsevier_sciencedirect_doi_10_1016_j_virusres_2011_03_015
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 2011-10-01
PublicationDateYYYYMMDD 2011-10-01
PublicationDate_xml – month: 10
  year: 2011
  text: 2011-10-01
  day: 01
PublicationDecade 2010
PublicationPlace Netherlands
PublicationPlace_xml – name: Netherlands
PublicationTitle Virus research
PublicationTitleAlternate Virus Res
PublicationYear 2011
Publisher Elsevier B.V
Publisher_xml – name: Elsevier B.V
References Yamada, Takahashi, Hoshino, Takahashi, Ichiyama, Nagashima, Tanaka, Okamoto (bib0165) 2009; 90
Niikura, Takamura, Kim, Kawai, Saijo, Morikawa, Kurane, Li, Takeda, Yasutomi (bib0100) 2002; 293
Okamoto (bib0105) 2007; 127
Bu, Mamedova, Tan, Xia, Jiang, Hegde (bib0020) 2008; 82
Takamura, Niikura, Li, Takeda, Kusagawa, Takebe, Miyamura, Yasutomi (bib0150) 2004; 11
Xing, Li, Miyazaki, Simon, Wall, Moore, Wang, Takeda, Wakita, Miyamura, Cheng (bib0160) 2010
Schofield, Glamann, Emerson, Purcell (bib0120) 2000; 74
Jameel, Zafrullah, Ozdener, Panda (bib0055) 1996; 70
Li, Yamakawa, Suzuki, Tatsumi, Razak, Uchida, Takeda, Miyamura (bib0095) 1997; 71
Bhella, Gatherer, Chaudhry, Pink, Goodfellow (bib0010) 2008; 82
Panda, Thakral, Rehman (bib0110) 2007; 17
Zhu, Zhang, Zhang, Zhou, Wang, Huang, Wang, Yang, Jiang, Cai, Wang, Ai, Hu, Tang, Yao, Yan, Xian, Wu, Li, Miao, Ng, Shih, Xia (bib0175) 2010; 376
Choi, Hutson, Estes, Prasad (bib0030) 2008; 105
He, Miao, Zheng, Wu, Xie, Tang, Zhang, Ng, Xia (bib0045) 2008; 89
Guu, Liu, Ye, Mata, Li, Yin, Zhang, Tao (bib0040) 2009; 106
Li, Tang, Seetharaman, Yang, Gu, Zhang, Du, Shih, Hew, Sivaraman, Xia (bib0075) 2009; 5
Emerson, Clemente-Casares, Moiduddin, Arankalle, Torian, Purcell (bib0035) 2006; 87
Bradley, Andjaparidze, Cook, McCaustland, Balayan, Stetler, Velazquez, Robertson, Humphrey, Kane (bib0015) 1988; 69
Li, Scotti, Miyamura, Takeda (bib0080) 2007; 81
Kalia, Chandra, Rahman, Sehgal, Jameel (bib0070) 2009; 83
Prasad, Hardy, Dokland, Bella, Rossmann, Estes (bib0115) 1999; 286
Schofield, Purcell, Nguyen, Emerson (bib0125) 2003; 22
Hsu, Singh, Ochoa, Manayani, Manchester, Schneemann, Reddy (bib0050) 2006; 349
Xing, Kato, Li, Takeda, Miyamura, Hammar, Cheng (bib0155) 1999; 265
Balayan, Andjaparidze, Savinskaya, Ketiladze, Braginsky, Savinov, Poleschuk (bib0005) 1983; 20
Kakani, Reade, Katpally, Smith, Rochon (bib0065) 2008; 82
Li, Takeda, Miyamura, Matsuura, Wang, Engvall, Hammar, Xing, Cheng (bib0090) 2005; 79
Li, Suzaki, Ami, Dhole, Miyamura, Takeda (bib0085) 2004; 22
Takahashi, Yamada, Hoshino, Takahashi, Ichiyama, Tanaka, Okamoto (bib0145) 2008; 153
Yamashita, Mori, Miyazaki, Cheng, Yoshimura, Unno, Shima, Moriishi, Tsukihara, Li, Takeda, Miyamura, Matsuura (bib0170) 2009; 106
Johne, Plenge-Bonig, Hess, Ulrich, Reetz, Schielke (bib0060) 2010; 91
Takahashi, Hoshino, Tanaka, Takahashi, Nishizawa, Okamoto (bib0140) 2008; 153
Shrestha, Scott, Joshi, Mammen, Thapa, Thapa, Myint, Fourneau, Kuschner, Shrestha, David, Seriwatana, Vaughn, Safary, Endy, Innis (bib0130) 2007; 356
Chen, Neill, Estes, Prasad (bib0025) 2006; 103
Sreenivasan, Arankalle, Sehgal, Pavri (bib0135) 1984; 65
Schofield (10.1016/j.virusres.2011.03.015_bib0125) 2003; 22
Li (10.1016/j.virusres.2011.03.015_bib0080) 2007; 81
Johne (10.1016/j.virusres.2011.03.015_bib0060) 2010; 91
Li (10.1016/j.virusres.2011.03.015_bib0095) 1997; 71
Yamashita (10.1016/j.virusres.2011.03.015_bib0170) 2009; 106
Takahashi (10.1016/j.virusres.2011.03.015_bib0145) 2008; 153
Takamura (10.1016/j.virusres.2011.03.015_bib0150) 2004; 11
Panda (10.1016/j.virusres.2011.03.015_bib0110) 2007; 17
Kalia (10.1016/j.virusres.2011.03.015_bib0070) 2009; 83
Zhu (10.1016/j.virusres.2011.03.015_bib0175) 2010; 376
Li (10.1016/j.virusres.2011.03.015_bib0085) 2004; 22
Schofield (10.1016/j.virusres.2011.03.015_bib0120) 2000; 74
Bradley (10.1016/j.virusres.2011.03.015_bib0015) 1988; 69
Li (10.1016/j.virusres.2011.03.015_bib0090) 2005; 79
Bhella (10.1016/j.virusres.2011.03.015_bib0010) 2008; 82
Choi (10.1016/j.virusres.2011.03.015_bib0030) 2008; 105
Chen (10.1016/j.virusres.2011.03.015_bib0025) 2006; 103
Emerson (10.1016/j.virusres.2011.03.015_bib0035) 2006; 87
Guu (10.1016/j.virusres.2011.03.015_bib0040) 2009; 106
Hsu (10.1016/j.virusres.2011.03.015_bib0050) 2006; 349
Bu (10.1016/j.virusres.2011.03.015_bib0020) 2008; 82
He (10.1016/j.virusres.2011.03.015_bib0045) 2008; 89
Balayan (10.1016/j.virusres.2011.03.015_bib0005) 1983; 20
Li (10.1016/j.virusres.2011.03.015_bib0075) 2009; 5
Xing (10.1016/j.virusres.2011.03.015_bib0160) 2010
Prasad (10.1016/j.virusres.2011.03.015_bib0115) 1999; 286
Kakani (10.1016/j.virusres.2011.03.015_bib0065) 2008; 82
Yamada (10.1016/j.virusres.2011.03.015_bib0165) 2009; 90
Xing (10.1016/j.virusres.2011.03.015_bib0155) 1999; 265
Takahashi (10.1016/j.virusres.2011.03.015_bib0140) 2008; 153
Sreenivasan (10.1016/j.virusres.2011.03.015_bib0135) 1984; 65
Jameel (10.1016/j.virusres.2011.03.015_bib0055) 1996; 70
Okamoto (10.1016/j.virusres.2011.03.015_bib0105) 2007; 127
Shrestha (10.1016/j.virusres.2011.03.015_bib0130) 2007; 356
Niikura (10.1016/j.virusres.2011.03.015_bib0100) 2002; 293
References_xml – year: 2010
  ident: bib0160
  article-title: Structure of hepatitis E virion-sized particle reveals an RNA-dependent viral assembly pathway
  publication-title: J. Biol. Chem.
– volume: 106
  start-page: 12986
  year: 2009
  end-page: 12991
  ident: bib0170
  article-title: Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 103
  start-page: 8048
  year: 2006
  end-page: 8053
  ident: bib0025
  article-title: X-ray structure of a native calicivirus: structural insights into antigenic diversity and host specificity
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 153
  start-page: 1703
  year: 2008
  end-page: 1713
  ident: bib0145
  article-title: Monoclonal antibodies raised against the ORF3 protein of hepatitis E virus (HEV) can capture HEV particles in culture supernatant and serum but not those in feces
  publication-title: Arch. Virol.
– volume: 11
  start-page: 628
  year: 2004
  end-page: 635
  ident: bib0150
  article-title: DNA vaccine-encapsulated virus-like particles derived from an orally transmissible virus stimulate mucosal and systemic immune responses by oral administration
  publication-title: Gene Ther.
– volume: 90
  start-page: 1880
  year: 2009
  end-page: 1891
  ident: bib0165
  article-title: ORF3 protein of hepatitis E virus is essential for virion release from infected cells
  publication-title: J. Gen. Virol.
– volume: 87
  start-page: 697
  year: 2006
  end-page: 704
  ident: bib0035
  article-title: Putative neutralization epitopes and broad cross-genotype neutralization of hepatitis E virus confirmed by a quantitative cell-culture assay
  publication-title: J. Gen. Virol.
– volume: 22
  start-page: 370
  year: 2004
  end-page: 377
  ident: bib0085
  article-title: Protection of cynomolgus monkeys against HEV infection by oral administration of recombinant hepatitis E virus-like particles
  publication-title: Vaccine
– volume: 89
  start-page: 245
  year: 2008
  end-page: 249
  ident: bib0045
  article-title: Putative receptor-binding sites of hepatitis E virus
  publication-title: J. Gen. Virol.
– volume: 71
  start-page: 7207
  year: 1997
  end-page: 7213
  ident: bib0095
  article-title: Expression and self-assembly of empty virus-like particles of hepatitis E virus
  publication-title: J. Virol.
– volume: 5
  start-page: e1000537
  year: 2009
  ident: bib0075
  article-title: Dimerization of hepatitis E virus capsid protein E2s domain is essential for virus–host interaction
  publication-title: PLoS Pathog.
– volume: 376
  start-page: 895
  year: 2010
  end-page: 902
  ident: bib0175
  article-title: Efficacy and safety of a recombinant hepatitis E vaccine in healthy adults: a large-scale, randomised, double-blind placebo-controlled, phase 3 trial
  publication-title: Lancet
– volume: 106
  start-page: 12992
  year: 2009
  end-page: 12997
  ident: bib0040
  article-title: Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 17
  start-page: 151
  year: 2007
  end-page: 180
  ident: bib0110
  article-title: Hepatitis E virus
  publication-title: Rev. Med. Virol.
– volume: 293
  start-page: 273
  year: 2002
  end-page: 280
  ident: bib0100
  article-title: Chimeric recombinant hepatitis E virus-like particles as an oral vaccine vehicle presenting foreign epitopes
  publication-title: Virology
– volume: 127
  start-page: 216
  year: 2007
  end-page: 228
  ident: bib0105
  article-title: Genetic variability and evolution of hepatitis E virus
  publication-title: Virus Res.
– volume: 70
  start-page: 207
  year: 1996
  end-page: 216
  ident: bib0055
  article-title: Expression in animal cells and characterization of the hepatitis E virus structural proteins
  publication-title: J. Virol.
– volume: 82
  start-page: 8051
  year: 2008
  end-page: 8058
  ident: bib0010
  article-title: Structural insights into calicivirus attachment and uncoating
  publication-title: J. Virol.
– volume: 81
  start-page: 10890
  year: 2007
  end-page: 10896
  ident: bib0080
  article-title: Latent infection of a new alphanodavirus in an insect cell line
  publication-title: J. Virol.
– volume: 22
  start-page: 257
  year: 2003
  end-page: 267
  ident: bib0125
  article-title: Monoclonal antibodies that neutralize HEV recognize an antigenic site at the carboxyterminus of an ORF2 protein vaccine
  publication-title: Vaccine
– volume: 82
  start-page: 5340
  year: 2008
  end-page: 5347
  ident: bib0020
  article-title: Structural basis for the receptor binding specificity of Norwalk virus
  publication-title: J. Virol.
– volume: 20
  start-page: 23
  year: 1983
  end-page: 31
  ident: bib0005
  article-title: Evidence for a virus in non-A, non-B hepatitis transmitted via the fecal–oral route
  publication-title: Intervirology
– volume: 349
  start-page: 222
  year: 2006
  end-page: 229
  ident: bib0050
  article-title: Characterization of polymorphism displayed by the coat protein mutants of tomato bushy stunt virus
  publication-title: Virology
– volume: 286
  start-page: 287
  year: 1999
  end-page: 290
  ident: bib0115
  article-title: X-ray crystallographic structure of the Norwalk virus capsid
  publication-title: Science
– volume: 79
  start-page: 12999
  year: 2005
  end-page: 13006
  ident: bib0090
  article-title: Essential elements of the capsid protein for self-assembly into empty virus-like particles of hepatitis E virus
  publication-title: J. Virol.
– volume: 83
  start-page: 12714
  year: 2009
  end-page: 12724
  ident: bib0070
  article-title: Heparan sulfate proteoglycans are required for cellular binding of the hepatitis E virus ORF2 capsid protein and for viral infection
  publication-title: J. Virol.
– volume: 91
  start-page: 750
  year: 2010
  end-page: 758
  ident: bib0060
  article-title: Detection of a novel hepatitis E-like virus in faeces of wild rats using a nested broad-spectrum RT-PCR
  publication-title: J. Gen. Virol.
– volume: 265
  start-page: 35
  year: 1999
  end-page: 45
  ident: bib0155
  article-title: Recombinant hepatitis E capsid protein self-assembles into a dual-domain
  publication-title: Virology
– volume: 153
  start-page: 657
  year: 2008
  end-page: 666
  ident: bib0140
  article-title: Production of monoclonal antibodies against hepatitis E virus capsid protein and evaluation of their neutralizing activity in a cell culture system
  publication-title: Arch. Virol.
– volume: 356
  start-page: 895
  year: 2007
  end-page: 903
  ident: bib0130
  article-title: Safety and efficacy of a recombinant hepatitis E vaccine
  publication-title: N. Engl. J. Med.
– volume: 105
  start-page: 9175
  year: 2008
  end-page: 9180
  ident: bib0030
  article-title: Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 82
  start-page: 1547
  year: 2008
  end-page: 1557
  ident: bib0065
  article-title: Induction of particle polymorphism by cucumber necrosis virus coat protein mutants in vivo
  publication-title: J. Virol.
– volume: 74
  start-page: 5548
  year: 2000
  end-page: 5555
  ident: bib0120
  article-title: Identification by phage display and characterization of two neutralizing chimpanzee monoclonal antibodies to the hepatitis E virus capsid protein
  publication-title: J. Virol.
– volume: 69
  start-page: 731
  year: 1988
  end-page: 738
  ident: bib0015
  article-title: Aetiological agent of enterically transmitted non-A, non-B hepatitis
  publication-title: J. Gen. Virol.
– volume: 65
  start-page: 1005
  year: 1984
  end-page: 1007
  ident: bib0135
  article-title: Non-A, non-B epidemic hepatitis: visualization of virus-like particles in the stool by immune electron microscopy
  publication-title: J. Gen. Virol.
– volume: 376
  start-page: 895
  year: 2010
  ident: 10.1016/j.virusres.2011.03.015_bib0175
  article-title: Efficacy and safety of a recombinant hepatitis E vaccine in healthy adults: a large-scale, randomised, double-blind placebo-controlled, phase 3 trial
  publication-title: Lancet
  doi: 10.1016/S0140-6736(10)61030-6
– volume: 105
  start-page: 9175
  year: 2008
  ident: 10.1016/j.virusres.2011.03.015_bib0030
  article-title: Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0803275105
– volume: 74
  start-page: 5548
  year: 2000
  ident: 10.1016/j.virusres.2011.03.015_bib0120
  article-title: Identification by phage display and characterization of two neutralizing chimpanzee monoclonal antibodies to the hepatitis E virus capsid protein
  publication-title: J. Virol.
  doi: 10.1128/JVI.74.12.5548-5555.2000
– volume: 87
  start-page: 697
  year: 2006
  ident: 10.1016/j.virusres.2011.03.015_bib0035
  article-title: Putative neutralization epitopes and broad cross-genotype neutralization of hepatitis E virus confirmed by a quantitative cell-culture assay
  publication-title: J. Gen. Virol.
  doi: 10.1099/vir.0.81545-0
– volume: 91
  start-page: 750
  year: 2010
  ident: 10.1016/j.virusres.2011.03.015_bib0060
  article-title: Detection of a novel hepatitis E-like virus in faeces of wild rats using a nested broad-spectrum RT-PCR
  publication-title: J. Gen. Virol.
  doi: 10.1099/vir.0.016584-0
– volume: 349
  start-page: 222
  year: 2006
  ident: 10.1016/j.virusres.2011.03.015_bib0050
  article-title: Characterization of polymorphism displayed by the coat protein mutants of tomato bushy stunt virus
  publication-title: Virology
  doi: 10.1016/j.virol.2006.02.038
– volume: 83
  start-page: 12714
  year: 2009
  ident: 10.1016/j.virusres.2011.03.015_bib0070
  article-title: Heparan sulfate proteoglycans are required for cellular binding of the hepatitis E virus ORF2 capsid protein and for viral infection
  publication-title: J. Virol.
  doi: 10.1128/JVI.00717-09
– volume: 20
  start-page: 23
  year: 1983
  ident: 10.1016/j.virusres.2011.03.015_bib0005
  article-title: Evidence for a virus in non-A, non-B hepatitis transmitted via the fecal–oral route
  publication-title: Intervirology
  doi: 10.1159/000149370
– volume: 82
  start-page: 1547
  year: 2008
  ident: 10.1016/j.virusres.2011.03.015_bib0065
  article-title: Induction of particle polymorphism by cucumber necrosis virus coat protein mutants in vivo
  publication-title: J. Virol.
  doi: 10.1128/JVI.01976-07
– volume: 89
  start-page: 245
  year: 2008
  ident: 10.1016/j.virusres.2011.03.015_bib0045
  article-title: Putative receptor-binding sites of hepatitis E virus
  publication-title: J. Gen. Virol.
  doi: 10.1099/vir.0.83308-0
– volume: 70
  start-page: 207
  year: 1996
  ident: 10.1016/j.virusres.2011.03.015_bib0055
  article-title: Expression in animal cells and characterization of the hepatitis E virus structural proteins
  publication-title: J. Virol.
  doi: 10.1128/JVI.70.1.207-216.1996
– volume: 65
  start-page: 1005
  issue: Pt 5
  year: 1984
  ident: 10.1016/j.virusres.2011.03.015_bib0135
  article-title: Non-A, non-B epidemic hepatitis: visualization of virus-like particles in the stool by immune electron microscopy
  publication-title: J. Gen. Virol.
  doi: 10.1099/0022-1317-65-5-1005
– volume: 5
  start-page: e1000537
  year: 2009
  ident: 10.1016/j.virusres.2011.03.015_bib0075
  article-title: Dimerization of hepatitis E virus capsid protein E2s domain is essential for virus–host interaction
  publication-title: PLoS Pathog.
  doi: 10.1371/journal.ppat.1000537
– volume: 82
  start-page: 5340
  year: 2008
  ident: 10.1016/j.virusres.2011.03.015_bib0020
  article-title: Structural basis for the receptor binding specificity of Norwalk virus
  publication-title: J. Virol.
  doi: 10.1128/JVI.00135-08
– volume: 106
  start-page: 12992
  year: 2009
  ident: 10.1016/j.virusres.2011.03.015_bib0040
  article-title: Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0904848106
– volume: 127
  start-page: 216
  year: 2007
  ident: 10.1016/j.virusres.2011.03.015_bib0105
  article-title: Genetic variability and evolution of hepatitis E virus
  publication-title: Virus Res.
  doi: 10.1016/j.virusres.2007.02.002
– volume: 265
  start-page: 35
  year: 1999
  ident: 10.1016/j.virusres.2011.03.015_bib0155
  article-title: Recombinant hepatitis E capsid protein self-assembles into a dual-domain T=1 particle presenting native virus epitopes
  publication-title: Virology
  doi: 10.1006/viro.1999.0005
– volume: 153
  start-page: 657
  year: 2008
  ident: 10.1016/j.virusres.2011.03.015_bib0140
  article-title: Production of monoclonal antibodies against hepatitis E virus capsid protein and evaluation of their neutralizing activity in a cell culture system
  publication-title: Arch. Virol.
  doi: 10.1007/s00705-008-0045-6
– year: 2010
  ident: 10.1016/j.virusres.2011.03.015_bib0160
  article-title: Structure of hepatitis E virion-sized particle reveals an RNA-dependent viral assembly pathway
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M110.106336
– volume: 103
  start-page: 8048
  year: 2006
  ident: 10.1016/j.virusres.2011.03.015_bib0025
  article-title: X-ray structure of a native calicivirus: structural insights into antigenic diversity and host specificity
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0600421103
– volume: 22
  start-page: 370
  year: 2004
  ident: 10.1016/j.virusres.2011.03.015_bib0085
  article-title: Protection of cynomolgus monkeys against HEV infection by oral administration of recombinant hepatitis E virus-like particles
  publication-title: Vaccine
  doi: 10.1016/j.vaccine.2003.08.004
– volume: 79
  start-page: 12999
  year: 2005
  ident: 10.1016/j.virusres.2011.03.015_bib0090
  article-title: Essential elements of the capsid protein for self-assembly into empty virus-like particles of hepatitis E virus
  publication-title: J. Virol.
  doi: 10.1128/JVI.79.20.12999-13006.2005
– volume: 71
  start-page: 7207
  year: 1997
  ident: 10.1016/j.virusres.2011.03.015_bib0095
  article-title: Expression and self-assembly of empty virus-like particles of hepatitis E virus
  publication-title: J. Virol.
  doi: 10.1128/JVI.71.10.7207-7213.1997
– volume: 17
  start-page: 151
  year: 2007
  ident: 10.1016/j.virusres.2011.03.015_bib0110
  article-title: Hepatitis E virus
  publication-title: Rev. Med. Virol.
  doi: 10.1002/rmv.522
– volume: 293
  start-page: 273
  year: 2002
  ident: 10.1016/j.virusres.2011.03.015_bib0100
  article-title: Chimeric recombinant hepatitis E virus-like particles as an oral vaccine vehicle presenting foreign epitopes
  publication-title: Virology
  doi: 10.1006/viro.2001.1240
– volume: 69
  start-page: 731
  issue: Pt 3
  year: 1988
  ident: 10.1016/j.virusres.2011.03.015_bib0015
  article-title: Aetiological agent of enterically transmitted non-A, non-B hepatitis
  publication-title: J. Gen. Virol.
  doi: 10.1099/0022-1317-69-3-731
– volume: 82
  start-page: 8051
  year: 2008
  ident: 10.1016/j.virusres.2011.03.015_bib0010
  article-title: Structural insights into calicivirus attachment and uncoating
  publication-title: J. Virol.
  doi: 10.1128/JVI.00550-08
– volume: 22
  start-page: 257
  year: 2003
  ident: 10.1016/j.virusres.2011.03.015_bib0125
  article-title: Monoclonal antibodies that neutralize HEV recognize an antigenic site at the carboxyterminus of an ORF2 protein vaccine
  publication-title: Vaccine
  doi: 10.1016/j.vaccine.2003.07.008
– volume: 90
  start-page: 1880
  year: 2009
  ident: 10.1016/j.virusres.2011.03.015_bib0165
  article-title: ORF3 protein of hepatitis E virus is essential for virion release from infected cells
  publication-title: J. Gen. Virol.
  doi: 10.1099/vir.0.010561-0
– volume: 106
  start-page: 12986
  year: 2009
  ident: 10.1016/j.virusres.2011.03.015_bib0170
  article-title: Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0903699106
– volume: 81
  start-page: 10890
  year: 2007
  ident: 10.1016/j.virusres.2011.03.015_bib0080
  article-title: Latent infection of a new alphanodavirus in an insect cell line
  publication-title: J. Virol.
  doi: 10.1128/JVI.00807-07
– volume: 153
  start-page: 1703
  year: 2008
  ident: 10.1016/j.virusres.2011.03.015_bib0145
  article-title: Monoclonal antibodies raised against the ORF3 protein of hepatitis E virus (HEV) can capture HEV particles in culture supernatant and serum but not those in feces
  publication-title: Arch. Virol.
  doi: 10.1007/s00705-008-0179-6
– volume: 356
  start-page: 895
  year: 2007
  ident: 10.1016/j.virusres.2011.03.015_bib0130
  article-title: Safety and efficacy of a recombinant hepatitis E vaccine
  publication-title: N. Engl. J. Med.
  doi: 10.1056/NEJMoa061847
– volume: 286
  start-page: 287
  year: 1999
  ident: 10.1016/j.virusres.2011.03.015_bib0115
  article-title: X-ray crystallographic structure of the Norwalk virus capsid
  publication-title: Science
  doi: 10.1126/science.286.5438.287
– volume: 11
  start-page: 628
  year: 2004
  ident: 10.1016/j.virusres.2011.03.015_bib0150
  article-title: DNA vaccine-encapsulated virus-like particles derived from an orally transmissible virus stimulate mucosal and systemic immune responses by oral administration
  publication-title: Gene Ther.
  doi: 10.1038/sj.gt.3302193
SSID ssj0006376
Score 2.256352
SecondaryResourceType review_article
Snippet Hepatitis E is acute hepatitis caused by infection of hepatitis E virus (HEV) via a fecal-to-oral or zoonotic route. HEV is a small, non-enveloped virus...
SourceID proquest
pubmed
crossref
fao
elsevier
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 59
SubjectTerms Animals
bacteria
Baculoviridae
Baculovirus
capsid
Capsid protein
Capsid Proteins - chemistry
Capsid Proteins - genetics
Capsid Proteins - metabolism
Crystal structure
genome
hepatitis E
Hepatitis E - virology
Hepatitis E virus
Hepatitis E virus - chemistry
Hepatitis E virus - genetics
Hepatitis E virus - physiology
Humans
Orthohepevirus A
Particle assembly
RNA
virion
Virion - chemistry
Virion - genetics
Virion - physiology
Virus Assembly
viruses
Title Structure of hepatitis E viral particle
URI https://dx.doi.org/10.1016/j.virusres.2011.03.015
https://www.ncbi.nlm.nih.gov/pubmed/21440590
https://www.proquest.com/docview/2000007099
https://www.proquest.com/docview/893989497
https://www.proquest.com/docview/902376425
Volume 161
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3dS8MwED-mIvgifq9-UUHwqVvWpO36KKJMxb3MgW8haRPdGNvQTfDFv927tPUDHD74UCjhDprL9e4XcvkdwGneUgJBmwl0hB6M-LYdKHwNmOJRznRic8euf9eNO31x8xA91OCiugtDZZVl7C9iuovW5UiztGZzOhg0ewhWiF2OdjCuzSPdYBcJeXnj_avMI-auwRwJByT97ZbwsPE6eJ5jJnopqTx5g1F73N8T1JJVk8Uw1KWjqw1YL3Gkf1586ibUzHgLVovOkm_bcNZzvLDzZ-NPrP9kqG56NnjxL30q6h3503KOO9C_ury_6ARlT4QgQ6Q0CxA_cMMR5zNlVCSsCRO0dkuoOI2zvGWJGjROLTPGcqZxDB8dq3ZmLO5cdMh3YXk8GZs6-AkPcUEwg2khhE5CxXIbtzOtDYKyPBIeRJUhZFYShlPfipGsKsOGsjKgJANKxiUa0IPmp960oMz4UyOt7Cx_LL7EuP6nbh0XRqpHjImy3wuJMc9tlFjiwUm1WhJ_GjoJUWMzmZO-O8JFdOyBv0AGgRyR06fJYpGUUU0RRj0P9gpn-JwwMdHRvd79f0ztANbCquKwdQjL6DjmCCHQTB87Hz-GlfPr2073A6_-AkE
linkProvider Elsevier
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3dS8MwED_mhuiL-L36WUHwqS5r-rE-iiib073MgW8haROdyDbmJvjfe9emQ8Hhgw-FEnLQ3F3vfiGX3wGcZ00ZIGjTngrRgxHftjyJrx6TPMyYik2Ws-s_9KL2ILh7Cp8qcF3ehaGyShv7i5ieR2s70rDabEyGw0YfwQqxy9EOJm_zuAI1YqcKq1C76nTbvUVAjnjeY47meyTw7aLw6-XHcDrHZPRu2Tz5JaMOub_nqBUjx8uRaJ6Rbjdhw0JJ96r42i2o6NE2rBbNJT934KKfU8POp9odG_dFU-n0bPju3rhU1_vmTuwyd2Fwe_N43fZsWwQvRbA08xBCcM0R6jOpZRgY7ceo8GYgoyRKs6YhdtAoMUxrw5nCMXxUJFupNrh5UT7fg-poPNJ1cGPuo00wiakgCFTsS5aZqJUqpRGXZWHgQFgqQqSWM5xaV7yJsjjsVZQKFKRAwbhABTrQWMhNCtaMPyWSUs_ih_0FhvY_ZetoGCGfMSyKQd8n0rx8r8RiB85Kawn8b-gwRI70eE7y-SkuAmQH3CVzEMsRP30SL5-SMCorwsDnwH7hDIsFExkdXe09-MfSTmGt_fhwL-47ve4hrPtlAWLzCKroRPoYEdFMnViP_wKK7QTy
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Structure+of+hepatitis+E+viral+particle&rft.jtitle=Virus+research&rft.au=Mori%2C+Yoshio&rft.au=Matsuura%2C+Yoshiharu&rft.date=2011-10-01&rft.issn=1872-7492&rft.eissn=1872-7492&rft.volume=161&rft.issue=1&rft.spage=59&rft_id=info:doi/10.1016%2Fj.virusres.2011.03.015&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0168-1702&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0168-1702&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0168-1702&client=summon