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Animal: RNA Viruses |
Institutes of Virology1 and Pathology3, School of Veterinary Medicine Hannover, Buenteweg 17, 30559 Hannover, Germany
Federal Research Centre for Virus Diseases of Animals, Institute for Diagnostic Virology, Boddenblick 5a, 17498 Insel Riems, Germany2
Author for correspondence: Irene Greiser-Wilke. Fax +49 511 953 8898. e-mail Irene.Greiser-Wilke{at}tiho-hannover.de
Bovine viral diarrhoea virus (BVDV) is a member of the genus Pestivirus within the family Flaviviridae. In this report, protein localization studies were performed to assess the mechanism for the release of mature virus particles from infected cells. Since BVDV is an enveloped virus, budding from either intra- or extracellular membranes is feasible. A prerequisite for the latter mechanism is the integration of viral glycoproteins into the host cell membrane. Using monoclonal antibodies (MAbs) directed against the viral envelope glycoproteins E2 and ERNS, no specific signals were detected on the surface of BVDV-infected cells by indirect fluorescence, confocal microscopy or fluorescence-activated cell sorter analyses. Furthermore, biotin-labelled cell surface proteins of virus-infected and non-infected cells were not detected by immunoprecipitation using MAbs directed against ERNS and E2 or the non-structural protein NS2-3. None of these proteins was detected on the cell surface. In addition, to analyse the intracellular localization of the two viral glycoproteins ERNS and E2 and the non-structural proteins NS2-3 and NS3, subcellular fractionation of virus-infected cells followed by radioimmunoprecipitation with the MAbs were performed. These results led to the conclusion that the BVDV envelope glycoproteins ERNS and E2 as well as the non-structural proteins NS2-3 and NS3 were almost quantitatively associated with intracellular membranes. These findings indicate that BVDV is released by budding into the cisternae of the endoplasmic reticulum and that there seems to be no correlation between the location and function of the analysed proteins.
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