title: In vivo and in vitro models of demyelinating disease: a phosphoprotein phosphatase in host cell endosomes dephosphorylating the nucleocapsid protein of coronavirus JHM.
abstract: We have identified a phosphoprotein phosphatase which dephosphorylates efficiently the NC protein of coronavirus JHM. The activity was found in L-2 murine fibroblasts, Wistar Furth rat neonatal brain extracts, Wistar Furth rat oligodendrocyte primary cells and in Roc-1 cells, an oligodendrocytic hybrid cell line. In both L-2 cells and Roc-1 cells the enzyme was found to be localized predominantly in the endosomal fraction. The enzyme is optimally active at pH 7.0 and has a requirement for Mn++ ions. This PPPase activity is distinguishable from acidic and alkaline phosphatases. In view of the specificity of the endosomal PPPase for the phosphory-lated NC protein it is hypothesized that this enzyme may have a function during early stages of coronavirus infection.
authors.affiliation: Department of Microbiology and Immunology, London, Ontario, Canada.
authors.forename: D V
authors.initials: DV
authors.lastname: Mohandas
authors.forename: S
authors.initials: S
authors.lastname: Dales
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology*; D002213:Capsid / Q000378:metabolism*; D002460:Cell Line; D002472:Cell Transformation, Viral; D003332:Coronaviridae; D003711:Demyelinating Diseases / Q000382:microbiology*; D007700:Kinetics; D007739:L Cells / Q000201:enzymology; D051379:Mice; D008954:Models, Biological; D006517:Murine hepatitis virus / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D009836:Oligodendroglia / Q000201:enzymology; D015388:Organelles / Q000201:enzymology*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D051381:Rats; D011920:Rats, Inbred WF; D013379:Substrate Specificity; D014758:Viral Core Proteins / Q000378:metabolism*
chemical_list: D014758:Viral Core Proteins; D010749:Phosphoprotein Phosphatases