Characterization of an RNA-dependent RNA polymerase activity associated with measles virus.
An RNA-dependent RNA polymerase activity has been found copurifying with measles virus infectivity and complement-fixing antigen in three Vero cell-grown variants of measles virus: the attenuated Edmonston B strain, the natural non-attenuated Edmonston strain, and a subacute sclerosing panencephalitis isolate, IP-3. Incubation of purified measles virions with immunoglobulin G derived from sera of monkeys hyperimmunized against measles specifically removes activity sedimenting in the density region of measles virions. The requirements of the reaction, which is RNase sensitive, are similar to those reported for other paramyxovirus-associated activities, including detergent, divalent cation, ribonucleoside triphosphates, and a reducing agent. The size classes of RNA synthesized correspond to those found in measles-infected cells, including 50, 35, and 16 to 20S. The product RNA of the Edmonston B virus-stimulated reaction was rendered RNase resistant by annealing with RNA extracted from purified Edmonston B virions. RNA from uninfected Vero cells was ineffective in the annealing reaction.
D000937:Antigen-Antibody Reactions; D002474:Cell-Free System; D007074:Immunoglobulin G; D008459:Measles virus / Q000201:enzymology*; D012316:RNA Nucleotidyltransferases / Q000378:metabolism; D012367:RNA, Viral / Q000096:biosynthesis; D012324:RNA-Dependent RNA Polymerase / Q000276:immunology / Q000378:metabolism; D013190:SSPE Virus / Q000201:enzymology*
D007074:Immunoglobulin G; D012367:RNA, Viral; D012316:RNA Nucleotidyltransferases; D012324:RNA-Dependent RNA Polymerase