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PubMed1993

The current status of Leishmania RNA virus I.

Viruses of Leishmania have recently been identified and characterized. These viruses are consistently double-stranded RNA viruses of approximately 5 kb. They have not been shown to exist outside their protozoan host, persistently infecting these parasites. The laboratory of jean Patterson has been interested in characterizing and identifying viruses of protozoans in order to use them as molecular probes of the unique gene expression mechanisms of protozoan parasites.

Journal Article↗
PubMed1997

Peptidyl-transferase inhibitors have antiviral properties by altering programmed -1 ribosomal frameshifting efficiencies: development of model systems.

The effects of two peptidyl-transferase inhibitors, anisomycin and sparsomycin, on ribosomal frameshifting efficiencies and the propagation of yeast double-stranded RNA viruses were examined. At sublethal doses in yeast cells these drugs specifically alter the efficiency of -1, but not of +1, ribosomal frameshifting. These compounds promote loss of the yeast L-A double-stranded RNA virus, which uses a programmed -1 ribosomal frameshift to produce its Gag-Pol fusion protein. Both of these drugs also change the efficiency of -1 ribosomal frameshifting in yeast and mammalian in vitro translation systems, suggesting that they may have applications to control the propagation of viruses of higher eukaryotes, which also use this translational regulatory mechanism. Our results offer a new set of antiviral agents that may potentially have a broad range of applications in the clinical, veterinary, and agricultural fields.

Anisomycin↗
PubMed1980

Comparison of the Structure of C- and N-Polyhedrins from Two Occluded Viruses Pathogenic for Orgyia pseudotsugata.

C-and N-polyhedrins from a cytoplasmic polyhedrosis virus (a double-stranded RNA virus) and a nuclear polyhedrosis virus (a DNA virus), respectively, of Orgyia pseudotsugata were compared. Although both polyhedrins appear to stabilize their respective virions and have similar molecular weights, they differed in amino acid composition, tryptic peptide elution profiles from a cation-exchange resin, and N-terminal amino acid sequence and showed no antigenic relatedness. This suggests that these two proteins originated independently of one another.

Journal Article↗
PubMedDate not supplied

Successful treatment of decompensated chronic viral hepatitis by bursal disease virus vaccine.

Three cases of women with chronic liver inflammation caused by hepatitis B (two) and C (one) viral infections, were followed up to twelve years after diagnosis. As conventional therapy was ineffective and the patients progressed into decompensated liver disease, they were superinfected with massive doses of an attenuated variant (MTH-68/B) of the apathogenic avian Bursal Disease virus (a double-stranded RNA virus from the Birnaviridae family). Clinical symptoms and biochemical abnormalities were resolved in two patients following few months of virus treatment. Cirrhosis was stabilized and significant clinical improvement was achieved in the third patient--who before the virus therapy was moribund with recurring, diuretic-resistant ascites, variceal bleedings, portal encephalopathy and renal failure. To our knowledge, these are the first recorded cases of decompensated chronic viral hepatitis which went to long-lasting remission or were stabilized by superinfection with an apathogenic virus.

Adult↗
PubMed1988

Involvement of structural and nonstructural polypeptides on rotavirus RNA synthesis.

Rotavirus are segmented double stranded RNA viruses with a double protein capsid around a central core. The virus replicates in the cell cytoplasm. After infection, eleven mRNAs are transcribed from the viral genome. To characterize further the infection cycle, viral polypeptide synthesis and RNA replication were studied using labelled precursors. The involvement of nonstructural polypeptides NS34 and NS35 was determined by the kinetics of the appearance of viral polypeptides in infected cells. Experiments in which cycloheximide was used showed that the synthesis of both polypeptides was required to begin RNA replication. The isolation of subviral particles at 8 hours postinfection indicates that there is a particle containing the nonstructural polypeptides and the structural polypeptides VP1, VP2, and VP6 that seem to be able to transcribe the viral genome to produce other RNA species. The results suggest that there is a core-like particle similar to one obtained in vitro which upon the addition of VP6 is able to transcribe the virus genome. This seems to indicate that core-like particles may alter their specificity for plus or minus RNA synthesis depending upon the polypeptides that interact with it. The interaction between VP6 and the viral core was analyzed by means of antibodies raised against the viral core and VP6. The results suggest that VP6 contains a specific binding site to the core complex and this interaction allows the synthesis of mRNA.

Capsid↗
PubMed1998

The Gag domain of the Gag-Pol fusion protein directs incorporation into the L-A double-stranded RNA viral particles in Saccharomyces cerevisiae.

The L-A double-stranded RNA virus of yeast encodes its major coat protein, Gag, and a Gag-Pol fusion protein made by a -1 ribosomal frameshift, a coding strategy used by many retroviruses. We find that cells expressing only Gag from one plasmid and only Gag-Pol (in frame) from a separate plasmid can support the propagation of M1 double-stranded RNA, encoding the killer toxin. We use this system to separately investigate the functions of Gag and the Gag part of Gag-Pol. L-A contains two fusion protein molecules per particle, and although N-terminal acetylation of Gag is essential for viral assembly, it is completely dispensable for function of Gag-Pol. In general, the requirements on Gag for viral assembly and propagation are more stringent than on the Gag part of Gag-Pol. Finally, we directly show that it is Gag that instructs the incorporation of Gag-Pol into the viral particles.

Fusion Proteins, gag-pol↗
PubMed1987

Virus-encoded toxin of Ustilago maydis: two polypeptides are essential for activity.

Cells of Ustilago maydis containing double-stranded RNA viruses secrete a virus-encoded toxin to which other cells of the same species and related species are sensitive. Mutants affected in the expression of the KP6 toxin were characterized, and all were viral mutants. A temperature-sensitive nonkiller mutant indicated that the toxin consists of two polypeptides, 12.5K and 10K, that are essential for the toxic activity. The temperature-sensitive nonkiller mutant was affected in the expression of the 10K polypeptide, and its toxic activity was restored by the addition of the 10K polypeptide to its secreted inactive toxin. These results led to the reexamination of other mutants that were known to complement in vitro. Each was found to secrete one of the two polypeptides. Here we show for the first time that P6 toxin consists of two polypeptides that do not interact in solution, but both are essential for the toxic effect. Studies on the interaction between the two polypeptides indicated that there are no covalent or hydrogen bonds between the polypeptides. Toxin activity is not affected by the presence of 0.3 M NaCl in the toxin preparations and in the medium, suggesting that no electrostatic forces are involved in this interaction. Also, the two polypeptides do not share common antigenic determinants. The activity of the two polypeptides appears to be dependent on a sequential interaction with the target cell, and it is the 10K polypeptide that initiates the toxic effect. The similarity of the U. maydis virus-encoded toxin to that of Saccharomyces cerevisiae is discussed.

Basidiomycota↗
PubMed1999

Cryphonectria hypovirus 3, a virus species in the family hypoviridae with a single open reading frame.

Isolate Grand Haven (GH) 2 is a naturally occurring isolate of the chestnut blight fungus, Cryphonectria parasitica, that is greatly reduced in virulence due to the presence of a double-stranded RNA virus. Unlike many other virus-infected, hypovirulent isolates, GH2 is not substantially reduced in pigmentation, conidiation, or laccase expression compared to its virus-free counterpart. The dsRNA genome of the GH2 virus was cloned, sequenced, and compared to hypovirulence-associated viruses of the family Hypoviridae. GH2 dsRNA is considerably smaller than previously characterized members of the family, 9.8 kb compared to 12.5-12.7 kb for other members. The genome organization of GH2 dsRNA reflected the substantial difference in genome size. Like other members of the family, one strand contained a poly(A)(+) tail at the 3' end and a long sequence with several minicistrons at the 5' end of the same strand. Only a single open reading frame (ORF) of 8622 nucleotides was predicted from deduced translations of the poly(A)(+)-containing strand, however. This contrasts with the two-ORF structures of previously characterized members. Analysis of the deduced ORF of GH2 dsRNA revealed putative proteinase, RNA polymerase, and helicase domains similar to those previously identified in confirmed members of the virus family Hypoviridae. GH2 dsRNA was more distantly related to Cryphonectria hypovirus (CHV) 1-EP713 and CHV2-NB58 than the latter two were to each other but has features in common with each of those viruses. We propose that the GH2 virus be included in this taxon as a member of the genus Hypovirus, representing a strain of a new species, CHV3.

Amino Acid Sequence↗
PubMedDate not supplied

Structure and nuclear localization signal of the SKI3 antiviral protein of Saccharomyces cerevisiae.

The yeast chromosomal genes SKI2, SKI3, SKI4, SKI6, SKI7 and SKI8 repress the replication of double-stranded RNA viruses, protecting the host from the otherwise lethal effects of the virus. We cloned and sequenced the SKI3 gene and found that it encodes a 163 kDa protein including a typical nuclear localization signal. Cell fractionation experiments show that the SKI3 gene product is indeed tightly associated with nuclei and that the putative nuclear localization sequence directs beta-galactosidase into the nucleus. However, fusion of a part of the SKI3 protein lacking this signal with beta-galactosidase also directs beta-galactosidase into the nucleus, suggesting the presence of a second nuclear localization signal. The SKI3 gene is only essential in the presence of an M double-stranded RNA virus.

Amino Acid Sequence↗
PubMed1990

Circular single-stranded RNA replicon in Saccharomyces cerevisiae.

Circular RNA replicons have been reported in plants and, in one case, in animal cells. We describe such an element in yeast. In certain yeast strains, a 20S RNA species appears on transfer of cells to acetate medium. This phenotype shows cytoplasmic (non-Mendelian) inheritance and the 20S RNA is associated with 23-kDa protein subunits as a 32S particle. We demonstrate that yeast 20S RNA is an independent replicon with no homology to host genomic, mitochondrial, or 2-microns plasmid DNA or to the L-A, L-BC, or M1 double-stranded RNA viruses of yeast. The circularity of the 20S RNA is shown by the apparent absence of 3' and 5' ends, by two-dimensional gel electrophoresis, and by electron microscopy. Replication of yeast 20S RNA proceeds through an RNA-RNA pathway, and a 10,000-fold amplification occurs on shift to acetate medium. The copy number of 20S RNA is also reduced severalfold by the SKI gene products, a host antiviral system that also lowers the copy numbers of yeast double-stranded RNA viruses. Yeast 20S RNA and the hepatitis delta virus show some similarities.

Genotype↗
PubMed1981

Sequences at the 3' ends of yeast viral dsRNAs: proposed transcriptase and replicase initiation sites.

ScV is a double-stranded RNA virus of yeast consisting of two separately encapsidated dsRNAs (L and M). ScV-1 and ScV-2 are two dsRNA viruses present in two different yeast killer strains, K1 and K2. Our 3' end sequence analysis shows that the two sets of viral dsRNAs from ScV-1 and ScV-2 are very similar. Consensus sequences for transcriptase and replicase initiation are proposed. A stem and loop structure with a 3' terminal AUGC sequence, like that of several plant virus plus strand RNAs, is present at the putative replicase initiation site of one of the yeast viral RNA plus strands.

Base Sequence↗
PubMed2004

Mycocin production in Cryptococcus aquaticus.

Double-stranded RNA viruses of about 35 nm in diameter were isolated from a mycocin-secreting strain of Cryptococcus aquaticus. A derivative of this strain, lacking small dsRNA, was non-mycocinogenic and sensitive to its own toxin. The killing pattern of this mycocin was restricted to some species of the Cystofilobasidiales clade. Despite the differences in genome size of dsRNA viruses in mycocinogenic strains of Cryptococcus aquaticus, Cystofilobasidium sp. CBS 6569, Cystofilobasidium bisporidii, Cystofilobasidium infirmominiatum, Trichosporon pullulans and Xanthophyllomyces dendrorhous and killing patterns of their mycocins, the viral genomes showed homology in hybridisation experiments.

Cryptococcus↗
PubMed1995

Translation and M1 double-stranded RNA propagation: MAK18 = RPL41B and cycloheximide curing.

MAK18 is one of nearly 30 chromosomal genes of Saccharomyces cerevisiae necessary for propagation of the killer toxin-encoding M1 double-stranded RNA satellite of the L-A double-stranded RNA virus. We have cloned and sequenced MAK18 and find that it is identical to RPL41B, one of the two genes encoding large ribosomal subunit protein L41. The mak18-1 mutant is deficient in 60S subunits, which we suggest results in a preferential decrease in translation of viral poly(A)-deficient mRNA. We have reexamined the curing of M1 by low concentrations of cycloheximide (G. R. Fink and C. A. Styles, Proc. Natl. Acad. Sci. USA 69:2846-2849, 1972), which is known to act on ribosomal large subunit protein L29. We find that when M1 is supported by L-A proteins made from the poly(A)+ mRNA of a cDNA clone of L-A, cycloheximide does not decrease the M1 copy number, consistent with our hypothesis.

Cloning, Molecular↗
PubMed2006

Genetic reassortment of infectious bursal disease virus in nature.

Infectious bursal disease virus (IBDV), a double-stranded RNA virus, is a member of the Birnaviridae family. Four pathotypes of IBDV, attenuated, virulent, antigenic variant, and very virulent (vvIBDV), have been identified. We isolated and characterized the genomic reassortant IBDV strain ZJ2000 from severe field outbreaks in commercial flocks. Full-length genomic sequence analysis showed that ZJ2000 is a natural genetic reassortant virus with segments A and B derived from attenuated and very virulent strains of IBDV, respectively. ZJ2000 exhibited delayed replication kinetics as compared to attenuated strains. However, ZJ2000 was pathogenic to specific pathogen free (SPF) chickens and chicken embryos. Similar to a standard virulent IBDV strain, ZJ2000 caused 26.7% mortality, 100% morbidity, and severe bursal lesions at both gross and histopathological levels. Taken together, our data provide direct evidence for genetic reassortment of IBDV in nature, which may play an important role in the evolution, virulence, and host range of IBDV. Our data also suggest that VP2 is not the sole determinant of IBDV virulence, and that the RNA-dependent RNA polymerase protein, VP1, may play an important role in IBDV virulence. The discovery of reassortant viruses in nature suggests an additional risk of using live IBDV vaccines, which could act as genetic donors for genome reassortment.

Amino Acid Substitution↗