Analysis of the interaction between respiratory syncytial virus and lipid-rafts in Hep2 cells during infection
- MRC Virology Unit, Institute of Virology, Glasgow G11 5JR (United Kingdom)
- Institute of Cell and Molecular Biology, Biological Sciences EM Facility, University of Edinburgh, Edinburgh EH9 3JN (United Kingdom)
- IBLS Division of Virology, University of Glasgow, Institute of Virology, Glasgow G11 5JR (United Kingdom)
The assembly of respiratory syncytial virus (RSV) in lipid-rafts was examined in Hep2 cells. Confocal and electron microscopy showed that during RSV assembly, the cellular distribution of the complement regulatory proteins, decay accelerating factor (CD55) and CD59, changes and high levels of these cellular proteins are incorporated into mature virus filaments. The detergent-solubility properties of CD55, CD59, and the RSV fusion (F) protein were found to be consistent with each protein being located predominantly within lipid-raft structures. The levels of these proteins in cell-released virus were examined by immunoelectronmicroscopy and found to account for between 5% and 15% of the virus attachment (G) glycoprotein levels. Collectively, our findings suggest that an intimate association exists between RSV and lipid-raft membranes and that significant levels of these host-derived raft proteins, such as those regulating complement activation, are subsequently incorporated into the envelope of mature virus particles.
- OSTI ID:
- 20634874
- Journal Information:
- Virology, Vol. 327, Issue 2; Other Information: DOI: 10.1016/j.virol.2004.06.038; PII: S0042-6822(04)00396-4; Copyright (c) 2004 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0042-6822
- Country of Publication:
- United States
- Language:
- English
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