Abstract
In the double-shelled capsid of Phytoreovirus, the outer capsid attaches firmly to the 3-fold axes of the T = 1 core. It then forms a T = 13 lattice via lateral interactions among the P8 trimers (Wu et al., 2000, Virology 271, 18-25). Purified P8 molecules also assemble into hexagonal monolayers as well as tubular crystals. To explore the mechanisms of formation of these structures, the configurations of P8 trimers were compared and verified in particles of Rice dwarf virus and in tubular crystals (tubes) whose structure was determined by cryoelectron microscopy using helical reconstruction technique. Remarkable variations in intertrimer contacts were observed in the tubes and in the surface lattice of Rice dwarf virus capsid. Superposition of the atomic structure of P8 trimers in the structures analyzed by cryoelectron microscopy allowed us to identify groups of specific and stable interactions, some of which were preserved in the tubes and the quasi-equivalent T = 13 icosahedral lattice of the virion's shell. The flexible nature of the binding between P8 trimers, created via electrostatic interactions that hold radially inward, appears to allow the outer-capsid P8 trimers to envelop the ragged surface of the core, forming the double shell of an intact viral particle.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 252-265 |
| Number of pages | 14 |
| Journal | Journal of Molecular Biology |
| Volume | 383 |
| Issue number | 1 |
| DOIs | |
| State | Published - Oct 31 2008 |
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Keywords
- cryoelectron microscopy
- Phytoreovirus
- Rice dwarf virus
ASJC Scopus subject areas
- Virology
Cite this
Pleomorphic Configuration of the Trimeric Capsid Proteins of Rice dwarf virus that Allows Formation of Both the Outer Capsid and Tubular Crystals. / Iwasaki, Kenji; Miyazaki, Naoyuki; Hammar, Lena; Zhu, Yafeng; Omura, Toshihiro; Wu, Bomu; Sjöborg, Fredrik; Yonekura, Koji; Murata, Kazuyoshi; Namba, Keiichi; Caspar, Donald L.; Fujiyoshi, Yoshinori; Cheng, R. Holland.
In: Journal of Molecular Biology, Vol. 383, No. 1, 31.10.2008, p. 252-265.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Pleomorphic Configuration of the Trimeric Capsid Proteins of Rice dwarf virus that Allows Formation of Both the Outer Capsid and Tubular Crystals
AU - Iwasaki, Kenji
AU - Miyazaki, Naoyuki
AU - Hammar, Lena
AU - Zhu, Yafeng
AU - Omura, Toshihiro
AU - Wu, Bomu
AU - Sjöborg, Fredrik
AU - Yonekura, Koji
AU - Murata, Kazuyoshi
AU - Namba, Keiichi
AU - Caspar, Donald L.
AU - Fujiyoshi, Yoshinori
AU - Cheng, R. Holland
PY - 2008/10/31
Y1 - 2008/10/31
N2 - In the double-shelled capsid of Phytoreovirus, the outer capsid attaches firmly to the 3-fold axes of the T = 1 core. It then forms a T = 13 lattice via lateral interactions among the P8 trimers (Wu et al., 2000, Virology 271, 18-25). Purified P8 molecules also assemble into hexagonal monolayers as well as tubular crystals. To explore the mechanisms of formation of these structures, the configurations of P8 trimers were compared and verified in particles of Rice dwarf virus and in tubular crystals (tubes) whose structure was determined by cryoelectron microscopy using helical reconstruction technique. Remarkable variations in intertrimer contacts were observed in the tubes and in the surface lattice of Rice dwarf virus capsid. Superposition of the atomic structure of P8 trimers in the structures analyzed by cryoelectron microscopy allowed us to identify groups of specific and stable interactions, some of which were preserved in the tubes and the quasi-equivalent T = 13 icosahedral lattice of the virion's shell. The flexible nature of the binding between P8 trimers, created via electrostatic interactions that hold radially inward, appears to allow the outer-capsid P8 trimers to envelop the ragged surface of the core, forming the double shell of an intact viral particle.
AB - In the double-shelled capsid of Phytoreovirus, the outer capsid attaches firmly to the 3-fold axes of the T = 1 core. It then forms a T = 13 lattice via lateral interactions among the P8 trimers (Wu et al., 2000, Virology 271, 18-25). Purified P8 molecules also assemble into hexagonal monolayers as well as tubular crystals. To explore the mechanisms of formation of these structures, the configurations of P8 trimers were compared and verified in particles of Rice dwarf virus and in tubular crystals (tubes) whose structure was determined by cryoelectron microscopy using helical reconstruction technique. Remarkable variations in intertrimer contacts were observed in the tubes and in the surface lattice of Rice dwarf virus capsid. Superposition of the atomic structure of P8 trimers in the structures analyzed by cryoelectron microscopy allowed us to identify groups of specific and stable interactions, some of which were preserved in the tubes and the quasi-equivalent T = 13 icosahedral lattice of the virion's shell. The flexible nature of the binding between P8 trimers, created via electrostatic interactions that hold radially inward, appears to allow the outer-capsid P8 trimers to envelop the ragged surface of the core, forming the double shell of an intact viral particle.
KW - cryoelectron microscopy
KW - Phytoreovirus
KW - Rice dwarf virus
UR - http://www.scopus.com/inward/record.url?scp=52049123802&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=52049123802&partnerID=8YFLogxK
U2 - 10.1016/j.jmb.2008.08.021
DO - 10.1016/j.jmb.2008.08.021
M3 - Article
C2 - 18761354
AN - SCOPUS:52049123802
VL - 383
SP - 252
EP - 265
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 1
ER -