The birnavirus crystal structure reveals structural relationships among icosahedral viruses

Fasseli Joseph Coulibaly, Christophe Chevalier, Irina Gutsche, Joan Pous, Jorge Navaza, Stephane Bressanelli, Bernard Delmas, Felix A Rey

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Double-stranded RNA virions are transcriptionally competent icosahedral particles that must translocate across a lipid bilayer to function within the cytoplasm of the target cell. Birnaviruses are unique among dsRNA viruses as they have a single T = 13 icosahedral shell, lacking the characteristic inner capsid observed in the others. We determined the crystal structures of the T = 1 subviral particle (260 angstroms in diameter) and of the T = 13 intact virus particle (700 angstroms in diameter) of an avian birnavirus to 3 angstroms and 7 angstroms resolution, respectively. Our results show that VP2, the only component of the virus icosahedral capsid, is homologous both to the capsid protein of positive-strand RNA viruses, like the T = 3 nodaviruses, and to the T = 13 capsid protein of members of the Reoviridae family of dsRNA viruses. Together, these results provide important insights into the multiple functions of the birnavirus capsid and reveal unexpected structural relationships among icosahedral viruses.
Original languageEnglish
Pages (from-to)761 - 772
Number of pages12
JournalCell
Volume120
Issue number6
Publication statusPublished - 2005
Externally publishedYes

Cite this

Coulibaly, F. J., Chevalier, C., Gutsche, I., Pous, J., Navaza, J., Bressanelli, S., ... Rey, F. A. (2005). The birnavirus crystal structure reveals structural relationships among icosahedral viruses. Cell, 120(6), 761 - 772.
Coulibaly, Fasseli Joseph ; Chevalier, Christophe ; Gutsche, Irina ; Pous, Joan ; Navaza, Jorge ; Bressanelli, Stephane ; Delmas, Bernard ; Rey, Felix A. / The birnavirus crystal structure reveals structural relationships among icosahedral viruses. In: Cell. 2005 ; Vol. 120, No. 6. pp. 761 - 772.
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abstract = "Double-stranded RNA virions are transcriptionally competent icosahedral particles that must translocate across a lipid bilayer to function within the cytoplasm of the target cell. Birnaviruses are unique among dsRNA viruses as they have a single T = 13 icosahedral shell, lacking the characteristic inner capsid observed in the others. We determined the crystal structures of the T = 1 subviral particle (260 angstroms in diameter) and of the T = 13 intact virus particle (700 angstroms in diameter) of an avian birnavirus to 3 angstroms and 7 angstroms resolution, respectively. Our results show that VP2, the only component of the virus icosahedral capsid, is homologous both to the capsid protein of positive-strand RNA viruses, like the T = 3 nodaviruses, and to the T = 13 capsid protein of members of the Reoviridae family of dsRNA viruses. Together, these results provide important insights into the multiple functions of the birnavirus capsid and reveal unexpected structural relationships among icosahedral viruses.",
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Coulibaly, FJ, Chevalier, C, Gutsche, I, Pous, J, Navaza, J, Bressanelli, S, Delmas, B & Rey, FA 2005, 'The birnavirus crystal structure reveals structural relationships among icosahedral viruses' Cell, vol. 120, no. 6, pp. 761 - 772.

The birnavirus crystal structure reveals structural relationships among icosahedral viruses. / Coulibaly, Fasseli Joseph; Chevalier, Christophe; Gutsche, Irina; Pous, Joan; Navaza, Jorge; Bressanelli, Stephane; Delmas, Bernard; Rey, Felix A.

In: Cell, Vol. 120, No. 6, 2005, p. 761 - 772.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Coulibaly, Fasseli Joseph

AU - Chevalier, Christophe

AU - Gutsche, Irina

AU - Pous, Joan

AU - Navaza, Jorge

AU - Bressanelli, Stephane

AU - Delmas, Bernard

AU - Rey, Felix A

PY - 2005

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N2 - Double-stranded RNA virions are transcriptionally competent icosahedral particles that must translocate across a lipid bilayer to function within the cytoplasm of the target cell. Birnaviruses are unique among dsRNA viruses as they have a single T = 13 icosahedral shell, lacking the characteristic inner capsid observed in the others. We determined the crystal structures of the T = 1 subviral particle (260 angstroms in diameter) and of the T = 13 intact virus particle (700 angstroms in diameter) of an avian birnavirus to 3 angstroms and 7 angstroms resolution, respectively. Our results show that VP2, the only component of the virus icosahedral capsid, is homologous both to the capsid protein of positive-strand RNA viruses, like the T = 3 nodaviruses, and to the T = 13 capsid protein of members of the Reoviridae family of dsRNA viruses. Together, these results provide important insights into the multiple functions of the birnavirus capsid and reveal unexpected structural relationships among icosahedral viruses.

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Coulibaly FJ, Chevalier C, Gutsche I, Pous J, Navaza J, Bressanelli S et al. The birnavirus crystal structure reveals structural relationships among icosahedral viruses. Cell. 2005;120(6):761 - 772.