Skip to main content
ARS Home » Midwest Area » Ames, Iowa » National Animal Disease Center » Virus and Prion Research » Research » Publications at this Location » Publication #190001
Title: MATURATION OF BORNA DISEASE VIRUS GLYCOPROTEIN

Author
item EICKMANN, M - PHILIPPS UNIV, MARBURG
item KIERMAYER, S - PHILIPPS UNIV, MARBURG
item KRAUS, I - PHILIPPS UNIV, MARBURG
item GOSSL, M - PHILIPPS UNIV, MARBURG
item Richt, Juergen
item GARTEN, W - PHILIPPS UNIV, MARBURG

Submitted to: Federation of European Biochemical Societies Letters
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 7/19/2005
Publication Date: 8/1/2005
Citation: Eickmann, M., Kiermayer, S., Kraus, I., Gossl, M., Richt, J., Garten, W. 2005. Maturation of Borna disease virus glycoprotein. FEBS Lett. 579(21):4751-4756.

Interpretive Summary: Borna disease virus (BDV) causes a persistent infection of the central nervous system associated with non-protective immune responses. Borna disease is actually caused by side effects of the immune response to the viral infection, not by the virus itself. BDV can infect a wide range of warm-blooded animals with horses and sheep being the main natural hosts; there is speculation that BDV can also infect humans. This work describes the maturation of the surface glycoprotein (GP) of BDV. It was found that BDV-GP is mainly found in the endoplasmatic reticulum of infected cells and is present in a processed form in viral particles. This study contributes to our understanding of the role of viral glycoproteins in virus-induced brain diseases.

Technical Abstract: 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.