+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Cell-to-cell spread of Borna disease virus proceeds in the absence of the virus primary receptor and furin-mediated processing of the virus surface glycoprotein

Cell-to-cell spread of Borna disease virus proceeds in the absence of the virus primary receptor and furin-mediated processing of the virus surface glycoprotein

Journal of Virology 81(11): 5968-5977

Borna disease virus (BDV) is an enveloped virus with a nonsegmented negative-strand RNA genome whose organization is characteristic of Mononegavirales. BDV cell entry follows a receptor-mediated endocytosis pathway, which is initiated by the recognition of an as-yet-unidentified receptor at the cell surface by the virus glycoprotein G. BDV G is synthesized as a precursor (GPC) that is cleaved by the cellular protease furin to produce the mature glycoproteins GP1 and GP2, which have been implicated in receptor recognition and pH-dependent fusion events, respectively. BDV is highly neurotropic and its spread in cultured cells proceeds in the absence of detectable extracellular virus or syncytium formation. BDV spread has been proposed to be strictly dependent on the expression and correct processing of BDV G. Here we present evidence that cell-to-cell spread of BDV required neither the expression of cellular receptors involved in virus primary infection, nor the furin-mediated processing of BDV G. We also show that in furin-deficient cells, the release of BDV particles induced by the treatment of BDV-infected cells with hypertonic buffer was not significantly affected, while virion infectivity was dramatically impaired, correlating with the decreased incorporation of BDV G species into viral particles. These findings support the view that the propagation of BDV within the central nervous systems of infected hosts involves both a primary infection that follows a receptor-mediated endocytosis pathway and a subsequent cell-to-cell spread that is independent of the expression of the primary receptor and does not require the processing of BDV G into GP1 and GP2.

Please choose payment method:

(PDF emailed within 0-6 h: $19.90)

Accession: 015225186

Download citation: RISBibTeXText

PMID: 17376904

DOI: 10.1128/jvi.02426-06

Related references

Surface glycoprotein of Borna disease virus mediates virus spread from cell to cell. Cellular Microbiology 18(3): 340-354, 2016

Processing of the Borna disease virus glycoprotein gp94 by the subtilisin-like endoprotease furin. Journal of Virology 72(5): 4528-4533, 1998

Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface. Journal of Virology 83(23): 12622-5, 2009

Anti-idiotypic antibodies mimicking glycoprotein D of herpes simplex virus identify a cellular protein required for virus spread from cell to cell and virus-induced polykaryocytosis. Proceedings Of The National Academy Of Sciences Of The United States Of America. 93(5): 1836-1840, 1996

Borna disease virus-induced meningoencephalomyelitis caused by a virus-specific CD4+ T cell-mediated immune reaction. Journal of General Virology 71: 2565-2573, 1990

Inhibition of Borna disease virus-mediated cell fusion by monoclonal antibodies directed against the viral glycoprotein. Intervirology 47(2): 108-113, 2004

Characterization of Borna disease virus p56 protein, a surface glycoprotein involved in virus entry. Journal of Virology 71(4): 3208-3218, 1997

Borna disease virus induced meningoencephalomyelitis caused by a virus specific cd4 positive t cell mediated immune reaction. Journal of General Virology 71(11): 2565-2574, 1990

Measles virus spread by cell-cell contacts: uncoupling of contact-mediated receptor (CD46) downregulation from virus uptake. Journal of Virology 73(7): 5265-5273, 1999

Vaccine-induced antibodies to herpes simplex virus glycoprotein D epitopes involved in virus entry and cell-to-cell spread correlate with protection against genital disease in guinea pigs. Plos Pathogens 14(5): E1007095, 2018

N-terminal domain of Borna disease virus G (p56) protein is sufficient for virus receptor recognition and cell entry. Journal of Virology 75(15): 7078-7085, 2001

Borna disease virus induces acute fatal neurological disorders in neonatal gerbils without virus- and immune-mediated cell destructions. Virology 310(2): 245-253, 2003

Domains of herpes simplex virus I glycoprotein B that function in virus penetration, cell-to-cell spread, and cell fusion. Virology 186(1): 99-112, 1992

Glycoprotein gI of pseudorabies virus promotes cell fusion and virus spread via direct cell-to-cell transmission. Journal of Virology 66(4): 2316-2325, 1992

Varicella-zoster virus glycoprotein M homolog is glycosylated, is expressed on the viral envelope, and functions in virus cell-to-cell spread. Journal of Virology 82(2): 795-804, 2008