| First Author | Anastasia L | Year | 2008 |
| Journal | Biochim Biophys Acta | Volume | 1780 |
| Issue | 3 | Pages | 504-12 |
| PubMed ID | 18155174 | Mgi Jnum | J:136756 |
| Mgi Id | MGI:3796939 | Doi | 10.1016/j.bbagen.2007.11.011 |
| Citation | Anastasia L, et al. (2008) Over-expression of mammalian sialidase NEU3 reduces Newcastle disease virus entry and propagation in COS7 cells. Biochim Biophys Acta 1780(3):504-12 |
| abstractText | 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. |
