The small hydrophobic (SH) protein accumulates within lipid-raft structures of the Golgi complex during respiratory syncytial virus infection.
The cellular distribution of the small hydrophobic (SH) protein in respiratory syncytial virus (RSV)-infected cells was examined. Although the SH protein was distributed throughout the cytoplasm, it appeared to accumulate in the Golgi complex within membrane structures that were enriched in the raft lipid, GM1. The ability of the SH protein to interact with lipid-raft membranes was further confirmed by examining its detergent-solubility properties in Triton X-100 at 4 degrees C. This analysis showed that a large proportion of the SH protein exhibited detergent-solubility characteristics that were consistent with an association with lipid-raft membranes. Analysis of virus-infected cells by immuno-transmission electron microscopy revealed SH protein clusters on the cell surface, but only very low levels of the protein appeared to be associated with mature virus filaments and inclusion bodies. These data suggest that during virus infection, the compartments in the secretory pathway, such as the endoplasmic reticulum (ER) and Golgi complex, are major sites of accumulation of the SH protein. Furthermore, although a significant amount of this protein interacts with lipid-raft membranes within the Golgi complex, its presence within mature virus filaments is minimal.
Rixon
Helen W McL
HWM
MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK.
Brown
Gaie
G
MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK.
Aitken
James
J
Division of Virology, University of Glasgow, Institute of Virology, Church Street, Glasgow G11 5JR, UK.
McDonald
Terence
T
MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK.
Graham
Susan
S
MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK.
Sugrue
Richard J
RJ
MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK.
D000818:Animals; D002522:Chlorocebus aethiops; D005677:G(M1) Ganglioside / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D018357:Respiratory Syncytial Virus Infections / Q000378:metabolism*; D012136:Respiratory Syncytial Viruses / Q000378:metabolism*; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000032:analysis / Q000378:metabolism*; D014764:Viral Proteins / Q000032:analysis / Q000378:metabolism*
D014759:Viral Envelope Proteins; D014764:Viral Proteins; D005677:G(M1) Ganglioside