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PubMed1977

The properties of two recent isolates of cytoplasmic polyhedrosis viruses.

Cytoplasmic polyhedrosis viruses (CPVs) were isolated from laboratory cultures of Bombyx mori and Spodoptera exempta. The electrophoretic profile of the RNA segments of both viruses showed similarities with that of type 1 CPV. However, whereas the virus isolate from B. mori appeared identical to type 1 CPV (as assessed by serology, as well as the comparative mobilities of RNA segments and structural polypeptides), the isolate from S. exempta was distinct. Three of the ten viral RNA segments did not co-run with type 1 RNA, and the structural polypeptides of polyhedra had different molecular weights. It is proposed that the S. exempta isolate be included as a new 'type' (type 12) in a classification of these viruses.

Antigens, Viral↗
PubMed1979

Interference with polyhedral inclusion body (PIB) production in Trichoplusia ni cells infected with a high passage strain of Autographa californica nuclear polyhedrosis virus (NPV). Brief report.

Trichoplusia ni cells infected with a low passage (LP) strain of Autographa californica nuclear polyhedrosis virus (NPV) produce large numbers of polyhedral inclusion bodies (PIBs). Interference with PIB production occurs when T. ni cells are first inoculated with a high passage (HP) strain and then challenged with the LP strain. PIB production is reduced 100 fold to the level seen with HP virus infection only.

Cell Line↗
PubMed1977

Nucleoside triphosphate phosphohydrolase associated with cytoplasmic polyhedrosis virus.

Nucleoside triphosphate phosphohydrolase [EC 3.6.1.15] activity was found to be included in silkworm cytoplasmic polyhedrosis (CP) virus, which synthesizes mRNA carrying the 5'-terminal modification. This enzyme releases orthophosphate from the gamma-position in a nucleoside triphosphate, leaving nucleoside diphosphate. The rate of hydrolysis of ATP is faster than that of any other ribonucleoside triphosphate. Deoxy ATP is hydrolyzed rather faster than ATP. However, polynucleotides carrying triphosphate at the 5'-terminus, that is, 4S RNA which was synthesized by E. coli RNA polymerase [EC 2.7.7.6] using calf thymus DNA as a template, and the phage Q beta RNA (30S), are not effective substrates for this enzyme. Although the CP virion loses the viral genome and one kind of protein component on proteolytic treatment with pronase, the partially degraded virion still retains phosphohydrolase activity. The phosphohydrolase must therefore be associated firmly with the virion. This enzyme does not require the presence of nucleic acid for its function. Phosphohydrolysis of ATP by this enzyme activity represents a first step in the synthesis of the 5'-terminal modified mRNA of CP virus.

Adenosine Triphosphate↗