g(m1)-ganglioside and Newcastle-Disease

g(m1)-ganglioside has been researched along with Newcastle-Disease* in 1 studies

Other Studies

1 other study(ies) available for g(m1)-ganglioside and Newcastle-Disease

Article	Year
Over-expression of mammalian sialidase NEU3 reduces Newcastle disease virus entry and propagation in COS7 cells. Biochimica et biophysica acta, 2008, Volume: 1780, Issue:3 The paramyxovirus Newcastle Disease Virus (NDV) binds to sialic acid-containing glycoconjugates, sialoglycoproteins and sialoglycolipids (gangliosides) of host cell plasma membrane through its hemagglutinin-neuraminidase (sialidase) HN glycoprotein. We hypothesized that the modifications of the cell surface ganglioside pattern determined by over-expression of the mammalian plasma-membrane associated, ganglioside specific, sialidase NEU3 would affect the virus-host cell interactions. Using COS7 cells as a model system, we observed that over-expression of the murine MmNEU3 did not affect NDV binding but caused a marked reduction in NDV infection and virus propagation through cell-cell fusion. Moreover, since GD1a was greatly reduced in COS7 cells following NEU3-over-expression, we added [(3)H]-labelled GD1a to COS7 cells under conditions that block intralysosomal metabolic processing, and we observed a marked increase of GD1a cleavage to GM1 during NDV infection, indicating a direct involvement of the virus sialidase and host cell GD1a in NDV infectivity. Therefore, the decrease of GD1a in COS7 cell membrane upon MmNEU3 over-expression is likely to be instrumental to NDV reduced infection. Evidence was also provided for the preferential association of NDV-HN at 4 degrees C to detergent resistant microdomains (DRMs) of COS7 cells plasma membranes. Topics: Animals; Blotting, Western; Cell Fusion; Cell Membrane; Chlorocebus aethiops; Chromatography, Thin Layer; COS Cells; G(M1) Ganglioside; Gene Expression; Giant Cells; HN Protein; Neuraminidase; Newcastle Disease; Newcastle disease virus; Virus Internalization; Virus Replication	2008

Article

Year

Over-expression of mammalian sialidase NEU3 reduces Newcastle disease virus entry and propagation in COS7 cells.

Biochimica et biophysica acta, 2008, Volume: 1780, Issue:3

The paramyxovirus Newcastle Disease Virus (NDV) binds to sialic acid-containing glycoconjugates, sialoglycoproteins and sialoglycolipids (gangliosides) of host cell plasma membrane through its hemagglutinin-neuraminidase (sialidase) HN glycoprotein. We hypothesized that the modifications of the cell surface ganglioside pattern determined by over-expression of the mammalian plasma-membrane associated, ganglioside specific, sialidase NEU3 would affect the virus-host cell interactions. Using COS7 cells as a model system, we observed that over-expression of the murine MmNEU3 did not affect NDV binding but caused a marked reduction in NDV infection and virus propagation through cell-cell fusion. Moreover, since GD1a was greatly reduced in COS7 cells following NEU3-over-expression, we added [(3)H]-labelled GD1a to COS7 cells under conditions that block intralysosomal metabolic processing, and we observed a marked increase of GD1a cleavage to GM1 during NDV infection, indicating a direct involvement of the virus sialidase and host cell GD1a in NDV infectivity. Therefore, the decrease of GD1a in COS7 cell membrane upon MmNEU3 over-expression is likely to be instrumental to NDV reduced infection. Evidence was also provided for the preferential association of NDV-HN at 4 degrees C to detergent resistant microdomains (DRMs) of COS7 cells plasma membranes.

Topics: Animals; Blotting, Western; Cell Fusion; Cell Membrane; Chlorocebus aethiops; Chromatography, Thin Layer; COS Cells; G(M1) Ganglioside; Gene Expression; Giant Cells; HN Protein; Neuraminidase; Newcastle Disease; Newcastle disease virus; Virus Internalization; Virus Replication

2008