title: Three-dimensional structure of victorivirus HvV190S suggests coat proteins in most totiviruses share a conserved core.
abstract: Double-stranded (ds)RNA fungal viruses are currently assigned to six different families. Those from the family Totiviridae are characterized by nonsegmented genomes and single-layer capsids, 300-450 Å in diameter. Helminthosporium victoriae virus 190S (HvV190S), prototype of recently recognized genus Victorivirus, infects the filamentous fungus Helminthosporium victoriae (telomorph: Cochliobolus victoriae), which is the causal agent of Victoria blight of oats. The HvV190S genome is 5179 bp long and encompasses two large, slightly overlapping open reading frames that encode the coat protein (CP, 772 aa) and the RNA-dependent RNA polymerase (RdRp, 835 aa). To our present knowledge, victoriviruses uniquely express their RdRps via a coupled termination-reinitiation mechanism that differs from the well-characterized Saccharomyces cerevisiae virus L-A (ScV-L-A, prototype of genus Totivirus), in which the RdRp is expressed as a CP/RdRp fusion protein due to ribosomal frameshifting. Here, we used transmission electron cryomicroscopy and three-dimensional image reconstruction to determine the structures of HvV190S virions and two types of virus-like particles (capsids lacking dsRNA and capsids lacking both dsRNA and RdRp) at estimated resolutions of 7.1, 7.5, and 7.6 Å, respectively. The HvV190S capsid is thin and smooth, and contains 120 copies of CP arranged in a "T = 2" icosahedral lattice characteristic of ScV-L-A and other dsRNA viruses. For aid in our interpretations, we developed and used an iterative segmentation procedure to define the boundaries of the two, chemically identical CP subunits in each asymmetric unit. Both subunits have a similar fold, but one that differs from ScV-L-A in many details except for a core α-helical region that is further predicted to be conserved among many other totiviruses. In particular, we predict the structures of other victoriviruses to be highly similar to HvV190S and the structures of most if not all totiviruses including, Leishmania RNA virus 1, to be similar as well.
authors.affiliation: Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA, USA.
authors.forename: Sarah E
authors.initials: SE
authors.lastname: Dunn
authors.forename: Hua
authors.initials: H
authors.lastname: Li
authors.forename: Giovanni
authors.initials: G
authors.lastname: Cardone
authors.forename: Max L
authors.initials: ML
authors.lastname: Nibert
authors.forename: Said A
authors.initials: SA
authors.lastname: Ghabrial
authors.forename: Timothy S
authors.initials: TS
authors.lastname: Baker
mesh_terms: D036022:Capsid Proteins / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure*; D020285:Cryoelectron Microscopy; D016679:Genome, Viral / Q000235:genetics; D006375:Helminthosporium / Q000821:virology*; D021621:Imaging, Three-Dimensional; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D008968:Molecular Conformation; D016366:Open Reading Frames; D012330:RNA, Double-Stranded / Q000235:genetics; D012367:RNA, Viral / Q000235:genetics; D012324:RNA-Dependent RNA Polymerase / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D019197:Totivirus / Q000737:chemistry* / Q000235:genetics; D014771:Virion / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure
chemical_list: D036022:Capsid Proteins; D012330:RNA, Double-Stranded; D012367:RNA, Viral; D012324:RNA-Dependent RNA Polymerase