Abstract
The association of an RNA-dependent RNA polymerase activity with virions of pike fry rhabdovirus has been demonstrated by both in vitro and in vivo studies. The temperature optimum for the in vitro assay is around 20 C, although enzyme activity can be observed at 4 C. Preparations of pike fry virus possess a glycoprotein, a membrane protein, a nucleoprotein, an L protein, and a phosphoprotein, as well as an RNA of about 3.8 times 10-6 mol wt. A protein kinase activity has been found associated with virus preparations. In vitro RNA product analyses indicate that the virus-associated enzyme functions principally as a transcriptase synthesizing viral-complementary, heteropolymeric RNA.
MeSH Terms
Animals
Cell Line
Cell-Free System
Cricetinae
Cyprinidae
DNA-Directed RNA Polymerases/metabolism
Electrophoresis, Polyacrylamide Gel
Fishes/microbiology
Glycoproteins/biosynthesis
Kidney
Molecular Weight
Nucleoproteins/biosynthesis
Phosphoproteins/biosynthesis
Protein Kinases/metabolism
RNA Viruses/enzymology
RNA, Viral/biosynthesis
Temperature
Transcription, Genetic
Viral Plaque Assay
Viral Proteins/biosynthesis
Chemicals
Glycoproteins
Nucleoproteins
Phosphoproteins
RNA, Viral
Viral Proteins
Protein Kinases
DNA-Directed RNA Polymerases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Roy P
Clark H F
Madore H P
Bishop D H
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