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.
Highlights
The encapsidated, double-strandedRNA viruses infect a wide range of hosts including bacteria, plants, fungi, insects, and humans and other vertebrates [1,2]
The 3D cryo-reconstruction presented here of prototype victorivirus Helminthosporium victoriae virus 190S (HvV190S) approaches 7-Aresolution and shows the asymmetric unit of the capsid is a dimer comprising two, chemically identical coatprotein subunits organized in a so called ‘‘T = 2’’ lattice. These HvV190S subunits have a similar fold, but one that differs from Saccharomyces cerevisiae virus L-A (ScV-L-A) in many details except for a core ahelical region that is further predicted to be conserved among many other totiviruses
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
Summary
The encapsidated, double-stranded (ds)RNA viruses infect a wide range of hosts including bacteria, plants, fungi, insects, and humans and other vertebrates [1,2]. Fungal viruses have been touted as potentially beneficial, biological control agents of pathogenic fungi that infect economically important agricultural crops. This has added significance because fungicides in current use pose health hazards and environmental risks [4]. The capsids of all these viruses have an overall, spherical morphology and are constructed from an icosahedrally symmetric arrangement of one or more capsid proteins Most of these capsids are single-shelled and range in diameter from ,300 to ,450 A , with the exception of the larger, double-shelled reoviruses (600–850 A ) [4]. All dsRNA viruses, including those that infect fungi, must package one or more virally encoded RNA-dependent RNA polymerase (RdRp) molecules that replicate and transcribe the viral genome, since dsRNA cannot function as mRNA [1]
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