schliessen

Filtern

 

Bibliotheken

Cryo-EM structure of a novel calicivirus, Tulane virus.

Tulane virus (TV) is a newly isolated cultivatable calicivirus that infects juvenile rhesus macaques. Here we report a 6.3 #197; resolution cryo-electron microscopy structure of the TV virion. The TV virion is about 400 #197; in diameter and consists of a T = 3 icosahedral protein capsid enclosing t... Full description

Journal Title: PloS one 2013, Vol.8(3), p.e59817
Main Author: Yu, Guimei
Other Authors: Zhang, Dongsheng , Guo, Fei , Tan, Ming , Jiang, Xi , Jiang, Wen
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0059817
Link: http://search.proquest.com/docview/1321336640/?pq-origsite=primo
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: proquest1321336640
title: Cryo-EM structure of a novel calicivirus, Tulane virus.
format: Article
creator:
  • Yu, Guimei
  • Zhang, Dongsheng
  • Guo, Fei
  • Tan, Ming
  • Jiang, Xi
  • Jiang, Wen
subjects:
  • Caliciviridae–Ultrastructure
  • Capsid Proteins–Ultrastructure
  • Cryoelectron Microscopy–Methods
  • Capsid Proteins
ispartof: PloS one, 2013, Vol.8(3), p.e59817
description: Tulane virus (TV) is a newly isolated cultivatable calicivirus that infects juvenile rhesus macaques. Here we report a 6.3 #197; resolution cryo-electron microscopy structure of the TV virion. The TV virion is about 400 #197; in diameter and consists of a T = 3 icosahedral protein capsid enclosing the RNA genome. 180 copies of the major capsid protein VP1 (~57 KDa) are organized into two types of dimers A/B and C/C and form a thin, smooth shell studded with 90 dimeric protrusions. The overall capsid organization and the capsid protein fold of TV closely resemble that of other caliciviruses, especially of human Norwalk virus, the prototype human norovirus. These close structural similarities support TV as an attractive surrogate for the non-cultivatable human noroviruses. The most distinctive feature of TV is that its C/C dimers are in a highly flexible conformation with significantly reduced interactions between the shell (S) domain and the protruding (P) domain of VP1. A comparative structural analysis indicated that the P domains of TV C/C dimers were much more flexible than those of other caliciviruses. These observations, combined with previous studies on other caliciviruses, led us to hypothesize that the enhanced flexibility of C/C dimer P domains are likely required for efficient calicivirus-host cell interactions and the consequent uncoating and genome release. Residues in the S-P1 hinge between the S and P domain may play a critical role in the flexibility of P domains of C/C dimers.
language: eng
source:
identifier: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0059817
fulltext: fulltext
issn:
  • 19326203
  • 1932-6203
url: Link


@attributes
ID1895474774
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid1321336640
sourceidproquest
recordidTN_proquest1321336640
sourcesystemPC
pqid1321336640
galeid478165613
display
typearticle
titleCryo-EM structure of a novel calicivirus, Tulane virus.
creatorYu, Guimei ; Zhang, Dongsheng ; Guo, Fei ; Tan, Ming ; Jiang, Xi ; Jiang, Wen
contributorYu, Guimei (correspondence author) ; Yu, Guimei (record owner)
ispartofPloS one, 2013, Vol.8(3), p.e59817
identifierE-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0059817
subjectCaliciviridae–Ultrastructure ; Capsid Proteins–Ultrastructure ; Cryoelectron Microscopy–Methods ; Capsid Proteins
languageeng
source
descriptionTulane virus (TV) is a newly isolated cultivatable calicivirus that infects juvenile rhesus macaques. Here we report a 6.3 #197; resolution cryo-electron microscopy structure of the TV virion. The TV virion is about 400 #197; in diameter and consists of a T = 3 icosahedral protein capsid enclosing the RNA genome. 180 copies of the major capsid protein VP1 (~57 KDa) are organized into two types of dimers A/B and C/C and form a thin, smooth shell studded with 90 dimeric protrusions. The overall capsid organization and the capsid protein fold of TV closely resemble that of other caliciviruses, especially of human Norwalk virus, the prototype human norovirus. These close structural similarities support TV as an attractive surrogate for the non-cultivatable human noroviruses. The most distinctive feature of TV is that its C/C dimers are in a highly flexible conformation with significantly reduced interactions between the shell (S) domain and the protruding (P) domain of VP1. A comparative structural analysis indicated that the P domains of TV C/C dimers were much more flexible than those of other caliciviruses. These observations, combined with previous studies on other caliciviruses, led us to hypothesize that the enhanced flexibility of C/C dimer P domains are likely required for efficient calicivirus-host cell interactions and the consequent uncoating and genome release. Residues in the S-P1 hinge between the S and P domain may play a critical role in the flexibility of P domains of C/C dimers.
version9
lds50peer_reviewed
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
backlink$$Uhttp://search.proquest.com/docview/1321336640/?pq-origsite=primo$$EView_record_in_ProQuest_(subscribers_only)
search
creatorcontrib
0Yu, Guimei
1Zhang, Dongsheng
2Guo, Fei
3Tan, Ming
4Jiang, Xi
5Jiang, Wen
titleCryo-EM structure of a novel calicivirus, Tulane virus.
subject
0Caliciviridae–Ultrastructure
1Capsid Proteins–Ultrastructure
2Cryoelectron Microscopy–Methods
3Capsid Proteins
general
0English
110.1371/journal.pone.0059817
2MEDLINE (ProQuest)
3ProQuest Biological Science Collection
4ProQuest Natural Science Collection
5ProQuest SciTech Collection
6Biological Science Database
7Natural Science Collection
8SciTech Premium Collection
9Health Research Premium Collection
10Health Research Premium Collection (Alumni edition)
11Biological Science Index (ProQuest)
sourceidproquest
recordidproquest1321336640
issn
019326203
11932-6203
rsrctypearticle
creationdate2013
addtitlePloS one
searchscope
01007527
11007944
21009130
310000004
410000038
510000050
610000120
710000159
810000238
910000253
1010000260
1110000270
1210000271
1310000302
1410000350
15proquest
scope
01007527
11007944
21009130
310000004
410000038
510000050
610000120
710000159
810000238
910000253
1010000260
1110000270
1210000271
1310000302
1410000350
15proquest
lsr43
01007527false
11007944false
21009130false
310000004false
410000038false
510000050false
610000120false
710000159false
810000238false
910000253false
1010000260false
1110000270false
1210000271false
1310000302false
1410000350false
contributorYu, Guimei
startdate20130101
enddate20130101
citationpf e59817 pt e59817 vol 8 issue 3
lsr30VSR-Enriched:[galeid, pqid, description]
sort
titleCryo-EM structure of a novel calicivirus, Tulane virus.
authorYu, Guimei ; Zhang, Dongsheng ; Guo, Fei ; Tan, Ming ; Jiang, Xi ; Jiang, Wen
creationdate20130101
lso0120130101
facets
frbrgroupid3479546642767603081
frbrtype5
newrecords20181218
languageeng
creationdate2013
topic
0Caliciviridae–Ultrastructure
1Capsid Proteins–Ultrastructure
2Cryoelectron Microscopy–Methods
3Capsid Proteins
collection
0MEDLINE (ProQuest)
1ProQuest Biological Science Collection
2ProQuest Natural Science Collection
3ProQuest SciTech Collection
4Biological Science Database
5Natural Science Collection
6SciTech Premium Collection
7Health Research Premium Collection
8Health Research Premium Collection (Alumni edition)
9Biological Science Index (ProQuest)
prefilterarticles
rsrctypearticles
creatorcontrib
0Yu, Guimei
1Zhang, Dongsheng
2Guo, Fei
3Tan, Ming
4Jiang, Xi
5Jiang, Wen
jtitlePloS one
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext
addata
aulast
0Yu
1Zhang
2Guo
3Tan
4Jiang
aufirst
0Guimei
1Dongsheng
2Fei
3Ming
4Xi
5Wen
au
0Yu, Guimei
1Zhang, Dongsheng
2Guo, Fei
3Tan, Ming
4Jiang, Xi
5Jiang, Wen
addauYu, Guimei
atitleCryo-EM structure of a novel calicivirus, Tulane virus.
jtitlePloS one
risdate20130101
volume8
issue3
spagee59817
epagee59817
pagese59817
eissn1932-6203
formatjournal
genrearticle
ristypeJOUR
doi10.1371/journal.pone.0059817
urlhttp://search.proquest.com/docview/1321336640/
date2013-01-01