Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid

J 2013

Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid

NĚMEČEK, Daniel, Evžen BOURA, Weimin WU, Naiqian CHENG, Pavel PLEVKA et. al.

Základní údaje

Originální název

Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid

Autoři

NĚMEČEK, Daniel (203 Česká republika, garant, domácí), Evžen BOURA (203 Česká republika), Weimin WU (840 Spojené státy), Naiqian CHENG (840 Spojené státy), Pavel PLEVKA (203 Česká republika, domácí), Jian QIAO (840 Spojené státy), Leonard MINDICH (840 Spojené státy), J Bernard HEYMANN (840 Spojené státy), James H HURLEY (840 Spojené státy) a Alasdair C STEVEN (840 Spojené státy)

Vydání

Structure, CAMBRIDGE, CELL PRESS, 2013, 0969-2126

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 6.794

Kód RIV

RIV/00216224:14740/13:00069193

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.str.2013.06.007

UT WoS

000322927900013

Klíčová slova anglicky

Bacteriophage phi6; Cystoviridae; cryo-electron microscopy; capsid structure; capsid expansion; segmented genome; conformational change; RNA packaging

Štítky

ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 4. 4. 2014 11:11, Olga Křížová

Anotace

V originále

The cystovirus phi 6 shares several distinct features with other double-stranded RNA (dsRNA) viruses, including the human pathogen, rotavirus: segmented genomes, nonequivalent packing of 120 subunits in its icosahedral capsid, and capsids as compartments for transcription and replication. phi 6 assembles as a dodecahedral procapsid that undergoes major conformational changes as it matures into the spherical capsid. We determined the crystal structure of the capsid protein, P1, revealing a flattened trapezoid subunit with an alpha-helical fold. We also solved the procapsid with cryo-electron microscopy to comparable resolution. Fitting the crystal structure into the procapsid disclosed substantial conformational differences between the two P1 conformers. Maturation via two intermediate states involves remodeling on a similar scale, besides huge rigid-body rotations. The capsid structure and its stepwise maturation that is coupled to sequential packaging of three RNA segments sets the cystoviruses apart from other dsRNA viruses as a dynamic molecular machine.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

Citovat

NĚMEČEK, Daniel, Evžen BOURA, Weimin WU, Naiqian CHENG, Pavel PLEVKA, Jian QIAO, Leonard MINDICH, J Bernard HEYMANN, James H HURLEY a Alasdair C STEVEN. Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid. Structure. CAMBRIDGE: CELL PRESS, 2013, roč. 21, č. 8, s. 1374-1383. ISSN 0969-2126. Dostupné z: https://dx.doi.org/10.1016/j.str.2013.06.007.

@article{1121143,
   author = {Němeček, Daniel and Boura, Evžen and Wu, Weimin and Cheng, Naiqian and Plevka, Pavel and Qiao, Jian and Mindich, Leonard and Heymann, J Bernard and Hurley, James H and Steven, Alasdair C},
   article_location = {CAMBRIDGE},
   article_number = {8},
   doi = {http://dx.doi.org/10.1016/j.str.2013.06.007},
   keywords = {Bacteriophage phi6; Cystoviridae; cryo-electron microscopy; capsid structure; capsid expansion; segmented genome; conformational change; RNA packaging},
   language = {eng},
   issn = {0969-2126},
   journal = {Structure},
   title = {Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid},
   url = {http://www.ncbi.nlm.nih.gov/pubmed/23891288},
   volume = {21},
   year = {2013}
}

TY  - JOUR
ID  - 1121143
AU  - Němeček, Daniel - Boura, Evžen - Wu, Weimin - Cheng, Naiqian - Plevka, Pavel - Qiao, Jian - Mindich, Leonard - Heymann, J Bernard - Hurley, James H - Steven, Alasdair C
PY  - 2013
TI  - Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid
JF  - Structure
VL  - 21
IS  - 8
SP  - 1374-1383
EP  - 1374-1383
PB  - CELL PRESS
SN  - 09692126
KW  - Bacteriophage phi6
KW  - Cystoviridae
KW  - cryo-electron microscopy
KW  - capsid structure
KW  - capsid expansion
KW  - segmented genome
KW  - conformational change
KW  - RNA packaging
UR  - http://www.ncbi.nlm.nih.gov/pubmed/23891288
L2  - http://www.ncbi.nlm.nih.gov/pubmed/23891288
N2  - The cystovirus phi 6 shares several distinct features with other double-stranded RNA (dsRNA) viruses, including the human pathogen, rotavirus: segmented genomes, nonequivalent packing of 120 subunits in its icosahedral capsid, and capsids as compartments for transcription and replication. phi 6 assembles as a dodecahedral procapsid that undergoes major conformational changes as it matures into the spherical capsid. We determined the crystal structure of the capsid protein, P1, revealing a flattened trapezoid subunit with an alpha-helical fold. We also solved the procapsid with cryo-electron microscopy to comparable resolution. Fitting the crystal structure into the procapsid disclosed substantial conformational differences between the two P1 conformers. Maturation via two intermediate states involves remodeling on a similar scale, besides huge rigid-body rotations. The capsid structure and its stepwise maturation that is coupled to sequential packaging of three RNA segments sets the cystoviruses apart from other dsRNA viruses as a dynamic molecular machine.
ER  -

NĚMEČEK, Daniel, Evžen BOURA, Weimin WU, Naiqian CHENG, Pavel PLEVKA, Jian QIAO, Leonard MINDICH, J Bernard HEYMANN, James H HURLEY a Alasdair C STEVEN. Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid. \textit{Structure}. CAMBRIDGE: CELL PRESS, 2013, roč.~21, č.~8, s.~1374-1383. ISSN~0969-2126. Dostupné z: https://dx.doi.org/10.1016/j.str.2013.06.007.

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