title: Cryphonectria nitschkei virus 1 structure shows that the capsid protein of chrysoviruses is a duplicated helix-rich fold conserved in fungal double-stranded RNA viruses.
abstract: Cryoelectron microscopy reconstruction of Cryphonectria nitschkei virus 1, a double-stranded RNA (dsRNA) virus, shows that the capsid protein (60 copies/particle) is formed by a repeated helical core, indicative of gene duplication. This unusual organization is common to chrysoviruses. The arrangement of many of these putative α-helices is conserved in the totivirus L-A capsid protein, suggesting a shared motif. Our results indicate that a 120-subunit T=1 capsid is a conserved architecture that optimizes dsRNA replication and organization.
authors.affiliation: Department of Structure of Macromolecules, Centro Nacional de Biotecnología/CSIC, Campus Cantoblanco, Madrid, Spain.
authors.forename: Josué
authors.initials: J
authors.lastname: Gómez-Blanco
authors.forename: Daniel
authors.initials: D
authors.lastname: Luque
authors.forename: José M
authors.initials: JM
authors.lastname: González
authors.forename: José L
authors.initials: JL
authors.lastname: Carrascosa
authors.forename: Carlos
authors.initials: C
authors.lastname: Alfonso
authors.forename: Benes
authors.initials: B
authors.lastname: Trus
authors.forename: Wendy M
authors.initials: WM
authors.lastname: Havens
authors.forename: Said A
authors.initials: SA
authors.lastname: Ghabrial
authors.forename: José R
authors.initials: JR
authors.lastname: Castón
mesh_terms: D036022:Capsid Proteins / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012328:RNA Viruses / Q000737:chemistry* / Q000502:physiology; D012330:RNA, Double-Stranded / Q000096:biosynthesis; D012367:RNA, Viral / Q000096:biosynthesis; D020037:Sordariales / Q000821:virology*; D014779:Virus Replication / Q000502:physiology
chemical_list: D036022:Capsid Proteins; D012330:RNA, Double-Stranded; D012367:RNA, Viral