Analysis of the interaction between respiratory syncytial virus and lipid-rafts in Hep2 cells during infection.
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.
Brown
Gaie
G
MRC Virology Unit, Institute of Virology, Glasgow G11 5JR, UK.
Jeffree
Chris E
CE
McDonald
Terence
T
Rixon
Helen W McL
HW
Aitken
James D
JD
Sugrue
Richard J
RJ
D000818:Animals; D018958:CD55 Antigens / Q000378:metabolism*; D018957:CD59 Antigens / Q000378:metabolism*; D045744:Cell Line, Tumor; D002522:Chlorocebus aethiops; D006801:Humans; D021962:Membrane Microdomains / Q000737:chemistry / Q000378:metabolism*; D018613:Microscopy, Confocal; D008854:Microscopy, Electron; D018113:Respiratory Syncytial Virus, Human / Q000378:metabolism / Q000472:pathogenicity*; D014709:Vero Cells; D014771:Virion / Q000378:metabolism; D019065:Virus Assembly
D018958:CD55 Antigens; D018957:CD59 Antigens