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  • Maturation of Borna disease virus glycoprotein #MMPMID16098520
  • Eickmann M; Kiermayer S; Kraus I; Gossl M; Richt JA; Garten W
  • FEBS Lett 2005[Aug]; 579 (21): 4751-6 PMID16098520garesp_yesshow ga
  • The maturation of Borna disease virus (BDV) glycoprotein GP was studied in regard to intracellular compartmentalization, compartmentalization signal-domains, proteolytic processing, and packaging into virus particles. Our data show that BDV-GP is (i) predominantly located in the endoplasmic reticulum (ER), (ii) partially exists in the ER already as cleaved subunits GP-N and GP-C, (iii) is directed to the ER/cis-Golgi region by its transmembrane and/or cytoplasmic domains in CD8-BDV-GP hybrid constructs and (iv) is incorporated in the virus particles as authentic BDV glycoprotein exclusively in the cleaved form decorated with N-glycans of the complex type. Downregulation of BDV-glycoproteins on the cell surface, their limited proteolytic processing, and protection of antigenic epitopes on the viral glycoproteins by host-identical N-glycans are different strategies for persistent virus infections.
  • |Animals[MESH]
  • |Borna disease virus/*metabolism[MESH]
  • |COS Cells[MESH]
  • |Cercopithecus aethiops[MESH]
  • |Endoplasmic Reticulum/metabolism[MESH]
  • |Epitopes[MESH]
  • |Protein Structure, Tertiary[MESH]
  • |Protein Subunits/genetics/metabolism[MESH]
  • |Recombinant Fusion Proteins/genetics/metabolism[MESH]
  • |Viral Fusion Proteins/genetics/*metabolism[MESH]

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    4751 21.579 2005