Penicillium Stoloniferum Virus Research Articles

5′-Terminal phosphorylation and secondary structure of double-stranded RNA from a fungal virus

Different double-stranded RNA species from Penicillium stoloniferum virus have been phosphorylated at the 5′ termini with the aid of polynucleotide kinase. A very low phosphate uptake has been observed which, especially in the case of a relatively small molecular component, was increased several times by pretreatment with RNAase t 1. Adenosine and uridine have been detected at the 5′-termini of this RNA component. Digestion with RNAase T 1, an enzyme which does not cut across the two strands of a double-stranded RNA molecule, produced a new uridine terminus and increased the efficiency of phosphorylation. It is concluded that this double-stranded RNA molecule contains single-stranded stretches at or near the 5′-termini. The possibility of a circular structure being formed by the annealing of single-stranded tails is discussed.

Replication of double-stranded RNA in particles of Penicillium stoloniferum virus S.

RNA polymerase activity was assayed in different particle classes of Penicillium stoloniferum virus S. RNA polymerase activity was found to be associated with H particles, which contain double-stranded RNA and single-stranded RNA, but not with L particles, which contain only double-stranded RNA and not with M particles, which contain only single-stranded RNA. In H particles the reaction occurred with the formation of one new molecule of double-stranded RNA (or two complementary single strands of RNA) per virus particle and the production of product particles (P particles), which contained two molecules of double-stranded RNA (or its equivalent). This RNA polymerase is therefore a replicase, which catalyses the synthesis of the two complementary strands of double-stranded RNA in a single virus particle. This is the first report of this type of RNA polymerase system.

Capsid Polypeptides of Two Viruses Isolated from Penicillium stoloniferum

SUMMARY The capsid polypeptides of Penicillium stoloniferum virus S (PsV-S) and P. stoloniferum virus F (PsV-F) were examined by SDS-polyacrylamide gel electrophoresis. PsV-S contained one major (S2) and one minor (S1) polypeptide with mol. wt. 42500 and 55500, while PsV-F contained one major (F2) and one minor (F1) polypeptide with mol. wt. 47000 and 59000, respectively. Mol. wt. of S2 and F2 polypeptides calculated from amino acid analyses were 41500 and 48000, respectively. PsV-S capsid was estimated to contain 120 molecules of polypeptide S2 and 1 molecule of polypeptide S1.

Penicillium stoloniferum Virus: Large-Scale Concentration and Purification by Polyethylene Glycol

An experimental procedure developed to concentrate fungal viruses from large volumes of homogenized mycelia with water-soluble polymers, such as polyethylene glycol, possesses advantages over more conventional methods. Concentration of the Penicillium stoloniferum fast-moving virus from mycelial homogenates after addition of polyethylene glycol was rapid and produced large quantities of pure virus.

The Penicillium stoloniferum virus complex: Two similar double-stranded RNA virus-like particles in a single cell

Two electrophoretically and serologically distinct viruslike particles (PsV-f and PsV-s) were isolated from Penicillium stoloniferum Thom. ATCC No. 14586. They were purified by rate-zonal sucrose density-gradient centrifugation and separated by sucrose density-gradient electrophoresis at pH 8.0. Both preparations of viruslike particles were composed of several centrifugal and density components. Electron micrographs contained polyhedral particles with diameters of 34 nm. The viruslike particles with the highest electrophoretic mobility (PsV-f) contained three distinct classes of double-stranded RNA with molecular weights of 0.99, 0.89, and 0.23 × 10 6 daltons as well as single-stranded RNA. The PsV-s contained two double-stranded RNA classes with molecular weights of 1.01, and 0.94 × 10 6 daltons. All of twelve cultures grown from single spore isolates were found to contain both types of virus-like particles.