Advertisement

Coronaviruses pp 239-254 | Cite as

In Vivo and In Vitro Models of Demyelinating Disease XXI: Relationship Between Differentiation of RAT Oligodendrocytes and Control of JHMV Replication

  • Sven Beushausen
  • Samuel Dales
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 218)

Abstract

Coronavirus (CV) infection in the central nervous system (CNS) of rodents, first described by Bailey et al. (1), is under investigation by many laboratories as a model of virus-induced demyelinating disease (10, 25, 38). One of the most intriguing factors influencing the disease process in rats is the development of an age-related resistance to the neurotropic CV strain JHM virus (JHMV) which becomes manifested at about the time of weaning, when the animal is 3 weeks old and myelination of the CNS is being completed (37). When tested in vitro in primary expiants of neural cells from the neonatal rat CNS, replication of JHMV can be initiated in recently established oligodendrocyte cultures but is repressed in 3 week old cultures, coincident with their “time-clock” of differentiation. Experimentally manipulated differentiation of cultured oligodendrocytes by treatment with cAMP analogues such as N6, 2′ -0-dibutyryl-adenosine 3′:5′ -cyclic monphosphate (dbcAMP) or metabolites affecting the levels of cAMP also results in suppression of JHMV replication (3). This implies that metabolic events leading to the development towards the terminally differentiated cell may be involved in regulating virus expression. Control over virus expression by regulation of cAMP levels is not unique to either the CV or the oligodendrocyte: it has been shown to occur in other virus-cell systems, including infections of neuronal and non-neuronal cells by measles virus (24, 31, 46), and rat glial cells by rubella virus (41).

Keywords

Measle Virus Demyelinating Disease Nucleocapsid Protein Rubella Virus Cyclic Monophosphate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. 1.
    Bailey, O.T., Pappenheimer, A.M., Cheever, F.S., and J.B. Daniels. 1949. A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin. II. Pathology. J. Exp. Med. 90: 195–231.PubMedCrossRefGoogle Scholar
  2. 2.
    Barbarese, E., and S.E. Pfeiffer. 1981. Developmental regulation of myelin basic protein in dispersed cultures. Proc. NatL. Acad. Sci. USA 78: 1953–1957.PubMedCrossRefGoogle Scholar
  3. 3.
    Beushausen, S., and S. Dales. 1985. In vivo and in vitro models of demyelinating disease XI. Tropism and differentiation regulate the infectious process of coronaviruses in primary expiants of the rat CNS. Virology 141: 89–101.PubMedCrossRefGoogle Scholar
  4. 4.
    Bond, C.W., Anderson, K., and J.L. Leibowitz. 1984. Protein synthesis in cells infected by murine hepatitis virus JHM and A59: Tryptic peptide analysis. Arch. Virol. 80: 333–347.PubMedCrossRefGoogle Scholar
  5. 5.
    Cammer, W., Snyder, D.S., Zimmerman, T.R. Jr., Farooq, M., and W.T. Norton. 1982. Glycerol phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, and lactate dehydrogenase: Activities in oligodendrocytes, neurons, astrocytes, and myelin isolated from developing rat brains. J. Neurochem. 38: 360–367.PubMedCrossRefGoogle Scholar
  6. 6.
    Cheley, S., and R. Anderson. 1981. Cellular synthesis and modification of murine hepatitis virus polypeptides. J. gen. Virol. 54: 301–311.PubMedCrossRefGoogle Scholar
  7. 7.
    Cohen, P. 1982. The role of protein phosphorylation in neural and hormonal control of cellular activity. Nature (London) 296: 613–620.CrossRefGoogle Scholar
  8. 8.
    De Duve, C., Pressman, B.C., Gianelto, R., Wattiaux, R., and F. Appelmans. 1955. Tissue fractionation studies 6. Intracellular distribution of patterns of enzymes in rat-liver tissue. Biochem. J. 59: 59: 604–617.Google Scholar
  9. 9.
    Gilman, A.G., and M. Nirenberg. 1971. Effect of catecholamines on the adenosine 3′: 5′-cyclic monophosphate concentrations of clonal satellite cells of neurons. Proc. Natl. Acad. Sci. USA 68: 2165–2168.PubMedCrossRefGoogle Scholar
  10. 10.
    Hirano, N., Goto, N., Ogawa, T., Katsukiko, O., Murakami, T., and K. Fujinara. 1980. Hydrocephalus in suckling rats infected intracerebrally with mouse hepatitis virus, MHV-A59. Microbiol. Immunol. 24: 825–834.PubMedGoogle Scholar
  11. 11.
    Hoppe, J. 1985. cAMP-dependent protein kinases: conformational changes during activation. TIBS 10: 29–31.Google Scholar
  12. 12.
    Hsu, C.H., Morgan, E.M., and D.W. Kingsbury. 1982. Site-specific phosphorylation regulates the transcriptive activity of vesicular stomatitis virus NS protein. J. Virol. 43: 104–112.PubMedGoogle Scholar
  13. 13.
    Ingebritsen, T.S., and P. Cohen. 1983. Protein phosphatases: Properties and role in cellular regulation. Science (Washington) 221: 331–338.CrossRefGoogle Scholar
  14. 14.
    Kamata, T., and Y. Watanabe. 1977. Role of nucleocapsid protein phosphorylation in the transcription of influenza virus genome. Nature (London) 267: 460–462.CrossRefGoogle Scholar
  15. 15.
    Kingsford, L. and S.U. Emerson. 1980. Transcriptional activities of different phosphorylated species of NS protein purified from vesicular stomatitis virus and cytoplasm of infected cells. J. Virol. 33: 1097–1105.PubMedGoogle Scholar
  16. 16.
    Kondrashin, A. 1985. Cyclic AMP regulation and regulation of gene expression. TIBS 10: 97–98.Google Scholar
  17. 17.
    Krebs, E.G., and J.A. Beavo. 1979. Phosphorylation-dephosphorylation of enzymes. Ann. Rev. Biochem. 48: 923–959.PubMedCrossRefGoogle Scholar
  18. 18.
    Leis, J., Johnson, S., Collins, L.S., and J.A. Traugh. 1984. Effects of phosphorylation of avian retroviruses nucleocapsid protein pp12 on binding of viral RNA. J. Biol. Chem. 259: 7726–7732.PubMedGoogle Scholar
  19. 19.
    Lucas, A., Flintoff, W., Anderson, R., Percy, D., Coulter, M., and S. Dales. 1977. In vivo and in vitro models of dernyelinating diseases: Tropism of the JHM strain of murine hepatitis virus for cells of glial origin. Cell 12: 553–560.PubMedCrossRefGoogle Scholar
  20. 20.
    Massa, P.T., Wege, H., and V. ter Meulen. 1986. Analysis of murine hepatitis virus (JHM strain) tropism toward lewis rat glial cells in vitro. Type 1 astrocytes and brain macrophages (microglia) as primary glial cell targets. Lab. Invest. 55: 318–327.PubMedGoogle Scholar
  21. 21.
    McCarthy, K.D., and J. DeVellis. 1978. Alpha adrenergic receptor modulation of beta-adrenergic, adenosine and prostaglandin E1-.-increased adenosine 3′: 5′ cyclic monophosphate levels in primary cultures of glia. J. Cell. Nucl. Res. 4: 15–26.Google Scholar
  22. 22.
    McCarthy, K.D., and J. de Vellis. 1980. Preparation of separate astroglial and oligodendroglial cell cultures from rat cerebral tissue. J. Cell. Biol. 85: 890–902.PubMedCrossRefGoogle Scholar
  23. 23.
    McMorris, F.A. 1983. Cyclic AMP induction of the myelin enzyme 2′3′-cyclic nucleotide 3′-phosphohydrolase in rat oligodendrocytes. J. Neurochem. 41: 506–515.PubMedCrossRefGoogle Scholar
  24. 24.
    Miller, CA., and Carrigan, D.R. 1982. Reversible repression and activation of measles virus infection in neural cells. Proc. Natl. Acad. Sci. USA 79: 1629–1633.PubMedCrossRefGoogle Scholar
  25. 25.
    Nagashima, K., Wege, H., and V. ter Meulen. 1978. Early and late CNS effects of coronavi rus infection in rats. Adv. Exp. Med. Biol. 100: 395–409.PubMedCrossRefGoogle Scholar
  26. 26.
    Nairn, A.C., Hemmings, H.C. Jr., and P. Greengard. 1985. Protein kinases in the brain. Ann. Rev. Biochem. 54: 931–976.PubMedCrossRefGoogle Scholar
  27. 27.
    Nagashima, K., Wege, H., and V. ter Meulen. 1978. Early and late CNS effects of coronavirus infection in rats. Adv. Exp. Med. Biol. 100: 395–409.PubMedCrossRefGoogle Scholar
  28. 28.
    Paigen, K., and S. Griffiths. 1958. The intracellular location of phosphoprotein phosphatase activity. J. Biol. Chem. 234: 299–303.Google Scholar
  29. 29.
    Pfeiffer, S.E., Barbarese, E., and Bhat, S. 1981. Non-coordinate regulation of myelinogenic parameters in primary cultures of dissociated fetal rat brain. J. Neurosci. Res. 6: 369–380.PubMedCrossRefGoogle Scholar
  30. 30.
    Robbins, S.G., Frana, M.F., McGowan, J.J., Boyle, J.F. and K.V. Holmes. 1986. RNA-binding proteins of coronavirus MHV: Detection of monomeric and multimeric N protein with an RNA overlay-protein blot assay. Virology 150: 402–410.PubMedCrossRefGoogle Scholar
  31. 31.
    Robbins, S.J., and F. Rapp. 1980. Inhibition of measles virus replication by cyclic AMP. Virology 106: 317–326.PubMedCrossRefGoogle Scholar
  32. 32.
    Rogers, J.E., Narindrasorasak, S., Cates, G.A., and B.D. Sanwal. 1985. Regulation of protein kinase and its regulatory subunits during skeletal myogenesis. J. Biol. Chem. 260: 8002–8007.PubMedGoogle Scholar
  33. 33.
    Schlosnagle, D.C., Sander, E.G., Bazer, F.W., and R.M. Roberts. 1976. Requirement of an essential thiol group and ferric ion for the activity of the progesterone-induced porcine uterine purple phosphatase. J. Biol. Chem. 251: 4680–4685.PubMedGoogle Scholar
  34. 34.
    Schramm, M., and Z. Selinger. 1984. Message transmission: Receptor controlled adenylate cyclase system. Science (Washington, D.C.) 225: 13350–13356.CrossRefGoogle Scholar
  35. 35.
    Schwartz, D.A., and C.S. Rubin. 1983. Regulation of cAMP-dependent protein kinase subunit levels in friend erythroleukemic cells. J. Biol. Chem. 258: 777–784.PubMedGoogle Scholar
  36. 36.
    Sidell, S.G. 1982. Coronavirus JHM: Tryptic peptide fingerprinting of virion proteins and intracellular polypeptides. J. Gen. Virol. 62: 259–269.CrossRefGoogle Scholar
  37. 37.
    Sobue, G., and D. Pleasure. 1984. Schwann cell galactocerebroside is induced by derivatives of adenosine 3′: 5′-cyclic monophosphate. Science (Washington, D.C.) 224: 72–74.CrossRefGoogle Scholar
  38. 38.
    Sorensen, O., Percy, D., and S. Dales. 1980. In vivo and in vitro models of demyelinating diseases III. JHM virus infection of rats. Arch. Neurol. 37: 478–484.PubMedCrossRefGoogle Scholar
  39. 39.
    Steinberg, R.A., and D.A. Agard. 1981. Turnover of regulatory subunit of cAMP-dependent protein kinase in S49 mouse lymphoma cells. J. Biol. Chem. 256: 10731–10734.PubMedGoogle Scholar
  40. 40.
    Stohlman, S.A., and M.M.C. Lai. 1979. Phosphoproteins of murine hepatitis virus. J. Virol. 32: 672–675.PubMedGoogle Scholar
  41. 41.
    Van Alstyne, D., and Paty, D.W. 1983. The effect of dibutyryl cyclic AMP on restricted replication of rubella virus in rat glial cells in culture. Virology 124: 173–180.PubMedCrossRefGoogle Scholar
  42. 42.
    Walter, U., Costa, M.R., Breakfield, X.O., and P. Greengard. 1979. Presence of free cyclic AMP receptor protein and regulation of its level by cAMP in neuroblastoma-glioma hybrid cells. Proc. Natl. Acad. Sci. USA 76: 3251–3255.PubMedCrossRefGoogle Scholar
  43. 43.
    Wege, H., Muller, A., and V. ter Meulen. 1978. Genomic RNA of the murine coronavirus JHM. J. gen. Virol. 41: 217–227.PubMedCrossRefGoogle Scholar
  44. 44.
    Weldon, S.L., Mumby, M.C., and S.C. Taylor. 1985. The regulatory subunit of neural cAMP-dependent protein kinase II represents a unique gene product. J. Biol. Chem. 260: 6440–6448.PubMedGoogle Scholar
  45. 45.
    Wernicke, J.F., and J.J. Volpe. 1986. Gliai differentiation in dissociated cell cultures of neonatal rat brain: Non-coordinate and density-dependent regulation of oligodendroglial enzymes. J. Neurosci. Res. 15: 39–47.PubMedCrossRefGoogle Scholar
  46. 46.
    Yoshikawa, Y., and K. Yamanouchi. 1984. Effect of papaverine treatment on replication of measles virus in human neural and non-neural cells. J. Virol. 50: 489–496.PubMedGoogle Scholar
  47. 47.
    Zalin, R., J. 1977. Prostaglandins and Myoblast fusion. Dev. Biol. 59: 241–248.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Sven Beushausen
    • 1
  • Samuel Dales
    • 1
  1. 1.Cytobiology Group, Department of Microbiology and ImmunologyUniversity of Western OntarioLondonCanada

Personalised recommendations