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; Evžen BOURA; Weimin WU; Naiqian CHENG; Pavel PLEVKA; Jian QIAO; Leonard MINDICH; J Bernard HEYMANN; James H HURLEY a Alasdair C STEVEN

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

https://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://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 = {https://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://doi.org/10.1016/j.str.2013.06.007.

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