Heterodimers as the structural unit of the T=1 capsid of the fungal double-stranded RNA Rosellinia necatrix quadrivirus 1

Daniel Luque, Carlos P. Mata, Fernando González-Camacho, José M. González, Josué Gómez-Blanco, Carlos Alfonso, Germán Rivas, Wendy M. Havens, Satoko Kanematsu, Nobuhiro Suzuki, Said A. Ghabrial, Benes L. Trus, José R. Castón

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Most double-stranded RNA (dsRNA) viruses are transcribed and replicated in a specialized icosahedral capsid with a T=1 lattice consisting of 60 asymmetric capsid protein (CP) dimers. These capsids help to organize the viral genome and replicative complex( es). They also act as molecular sieves that isolate the virus genome from host defense mechanisms and allow the passage of nucleotides and viral transcripts. Rosellinia necatrix quadrivirus 1 (RnQV1), the type species of the family Quadriviridae, is a dsRNA fungal virus with a multipartite genome consisting of four monocistronic segments (segments 1 to 4). dsRNA-2 and dsRNA-4 encode two CPs (P2 and P4, respectively), which coassemble into~450-Å-diameter capsids. We used three-dimensional cryo-electron microscopy combined with complementary biophysical techniques to determine the structures of RnQV1 virion strains W1075 and W1118. RnQV1 has a quadripartite genome, and the capsid is based on a single-shelled T=1 lattice built of P2-P4 dimers. Whereas the RnQV1-W1118 capsid is built of full-length CP, P2 and P4 of RnQV1-W1075 are cleaved into several polypeptides, maintaining the capsid structural organization. RnQV1 heterodimers have a quaternary organization similar to that of homodimers of reoviruses and other dsRNA mycoviruses. The RnQV1 capsid is the first T=1 capsid with a heterodimer as an asymmetric unit reported to date and follows the architectural principle for dsRNA viruses that a 120-subunit capsid is a conserved assembly that supports dsRNA replication and organization.

Original languageEnglish
Pages (from-to)11220-11230
Number of pages11
JournalJournal of Virology
Volume90
Issue number24
DOIs
Publication statusPublished - 2016

Fingerprint

Fungal RNA
Rosellinia necatrix
capsid
Double-Stranded RNA
Capsid
double-stranded RNA
RNA Viruses
mycoviruses
dsRNA viruses
genome
Capsid Proteins
Genome
coat proteins
Cryoelectron Microscopy
Reoviridae
Viral Genome
sieves
virion
defense mechanisms
Virion

ASJC Scopus subject areas

  • Immunology
  • Virology

Cite this

Luque, D., Mata, C. P., González-Camacho, F., González, J. M., Gómez-Blanco, J., Alfonso, C., ... Castón, J. R. (2016). Heterodimers as the structural unit of the T=1 capsid of the fungal double-stranded RNA Rosellinia necatrix quadrivirus 1. Journal of Virology, 90(24), 11220-11230. https://doi.org/10.1128/JVI.01013-16

Heterodimers as the structural unit of the T=1 capsid of the fungal double-stranded RNA Rosellinia necatrix quadrivirus 1. / Luque, Daniel; Mata, Carlos P.; González-Camacho, Fernando; González, José M.; Gómez-Blanco, Josué; Alfonso, Carlos; Rivas, Germán; Havens, Wendy M.; Kanematsu, Satoko; Suzuki, Nobuhiro; Ghabrial, Said A.; Trus, Benes L.; Castón, José R.

In: Journal of Virology, Vol. 90, No. 24, 2016, p. 11220-11230.

Research output: Contribution to journalArticle

Luque, D, Mata, CP, González-Camacho, F, González, JM, Gómez-Blanco, J, Alfonso, C, Rivas, G, Havens, WM, Kanematsu, S, Suzuki, N, Ghabrial, SA, Trus, BL & Castón, JR 2016, 'Heterodimers as the structural unit of the T=1 capsid of the fungal double-stranded RNA Rosellinia necatrix quadrivirus 1', Journal of Virology, vol. 90, no. 24, pp. 11220-11230. https://doi.org/10.1128/JVI.01013-16
Luque, Daniel ; Mata, Carlos P. ; González-Camacho, Fernando ; González, José M. ; Gómez-Blanco, Josué ; Alfonso, Carlos ; Rivas, Germán ; Havens, Wendy M. ; Kanematsu, Satoko ; Suzuki, Nobuhiro ; Ghabrial, Said A. ; Trus, Benes L. ; Castón, José R. / Heterodimers as the structural unit of the T=1 capsid of the fungal double-stranded RNA Rosellinia necatrix quadrivirus 1. In: Journal of Virology. 2016 ; Vol. 90, No. 24. pp. 11220-11230.
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