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.

Basic information

Original name

Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid

Authors

NĚMEČEK, Daniel (203 Czech Republic, guarantor, belonging to the institution), Evžen BOURA (203 Czech Republic), Weimin WU (840 United States of America), Naiqian CHENG (840 United States of America), Pavel PLEVKA (203 Czech Republic, belonging to the institution), Jian QIAO (840 United States of America), Leonard MINDICH (840 United States of America), J Bernard HEYMANN (840 United States of America), James H HURLEY (840 United States of America) and Alasdair C STEVEN (840 United States of America)

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 6.794

RIV identification code

RIV/00216224:14740/13:00069193

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000322927900013

Keywords in English

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

Abstract

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.

Links

ED1.1.00/02.0068, research and development project

Name: 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 and Alasdair C STEVEN. Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid. Structure. CAMBRIDGE: CELL PRESS, 2013, vol. 21, No 8, p. 1374-1383. ISSN 0969-2126. Available from: 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 and Alasdair C STEVEN. Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid. \textit{Structure}. CAMBRIDGE: CELL PRESS, 2013, vol.~21, No~8, p.~1374-1383. ISSN~0969-2126. Available from: https://dx.doi.org/10.1016/j.str.2013.06.007.

Detailed Information on Publication Record