Cellular Processing of the Large Glycoprotein of Lacrosse Virus (Family Bunyaviridae); Implications for Virion Assembly and Host Defense

  • David H. Madoff
  • John Lenard
Conference paper
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 162)

Abstract

LaCrosse virus (LAC) is a major causative agent of mosquito-borne human encephalitis in the USA (1). LAC is an enveloped RNA virus containing two glycoproteins, Gl and G2 (2). Based on electron micrographs of LAC-infected cells, it is thought that LAC derives its lipid envelope by budding from host smooth membranes rather than from the plasma membrane (3). We have demonstrated that the LAC Gl protein accumulates in a juxtanuclear region (probably Golgi) and not at the plasma membrane of the infected cell. Further evidence suggests that Gl is inefficiently modified in Golgi (4).

Keywords

Saccharide EDTA Methionine Oligosaccharide Encephalitis 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Bishop, D.H.L. and Shope, R.E. (1979). Bunyaviridae. In: Comprehensive Virology, Vol. 14. H. Fraenkel-Conrat and R.R. Wagner, Eds. Plenum Press, New York, Chapter 1, pp. 1–156.Google Scholar
  2. 2.
    Obijeski, J.F., Bishop, D.H.L., Murphy, F.A. and Palmer, E.L. (1976). Structural proteins of LaCrosse virus. J. Virol. 19(3):985–997.PubMedGoogle Scholar
  3. 3.
    Murphy, F.A., Whitfield, S.G., Coleman, P.H., Calisher, C.H., Rabin, E.R., Jenson, A.B., Melnick, J.L., Edwards, M.R. and Whitney, E. (1968). California group arboviruses: Electron microscope studies, Exp. Mol. Path. 9:44–56.CrossRefGoogle Scholar
  4. 4.
    Madoff, D.H. and Lenard, J. (1982). A membrane glycoprotein that that accumulates intracellularly: Cellular processing of the large glycoprotein of La Crosse virus. Cell. 28, 821–829.PubMedCrossRefGoogle Scholar
  5. 5.
    Saraste, J., von Bonsdorff, C.-H., Hashimoto, K., Kääriäinen, L. and Keränen, S. (1980). Semliki forest virus mutants with temperature-sensitive transport defect of envelope proteins. Virology. 100:229–245.PubMedCrossRefGoogle Scholar
  6. 6.
    Vitranen, I., Ekblom, P. and Laurila, P. (1980). Subcellular compartmentalization of saccharide moieties in cultured normal and malignant cells. J. Cell Biol. 85:249–434.Google Scholar
  7. 7.
    Robbins, P.W., Hubbard, S.C., Turco, S.J. and Wirth, D.F. (1977). Proposal for a common oligosaccharide intermediate in the synthesis of membrane glycoproteins. Cell 12:893–900.PubMedCrossRefGoogle Scholar
  8. 8.
    Rothman, J.E. and Fries, E. (1981). Transport of newly synthesized vesicular stomatitis viral glycoprotein to purified Golgi membranes. J. Cell Biol. 89:162–168.PubMedCrossRefGoogle Scholar
  9. 9.
    Schmidt, M.F.G. and Schlessinger, M.J. (1980). Relation of fatty acid attachment to the translation and maturation of vesicular stomatitis and Sindbis virus membrane glycoproteins. J. Biol. Chem. 255(8):3334–3339.PubMedGoogle Scholar
  10. 10.
    Zilberstein, A., Snider, M.D., Porter, M. and Lodish, H.F. (1980). Mutants of vesicular stomatitis virus blocked at different stages in maturation of the viral glco-protein. Cell 21:417–427.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1983

Authors and Affiliations

  • David H. Madoff
    • 1
  • John Lenard
    • 1
  1. 1.Dept. of Physiology and BiophysicsUMDNJ-Rutgers Medical SchoolPiscatawayUSA

Personalised recommendations