| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK
2 Division of Virology, University of Glasgow, Institute of Virology, Church Street, Glasgow G11 5JR, UK
Correspondence
Richard J. Sugrue
r.sugrue{at}vir.gla.ac.uk
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 °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.
This article has been cited by other articles:
|
|
 |
|
  M. Batonick, A. G. P. Oomens, and G. W. Wertz Human Respiratory Syncytial Virus Glycoproteins Are Not Required for Apical Targeting and Release from Polarized Epithelial Cells J. Virol., September 1, 2008; 82(17): 8664 - 8672. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Fuentes, K. C. Tran, P. Luthra, M. N. Teng, and B. He Function of the Respiratory Syncytial Virus Small Hydrophobic Protein J. Virol., August 1, 2007; 81(15): 8361 - 8366. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. H. Fleming, A. A. Kolokoltsov, R. A. Davey, J. E. Nichols, and N. J. Roberts Jr. Respiratory Syncytial Virus F Envelope Protein Associates with Lipid Rafts without a Requirement for Other Virus Proteins J. Virol., December 15, 2006; 80(24): 12160 - 12170. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. P. Laliberte, L. W. McGinnes, M. E. Peeples, and T. G. Morrison Integrity of membrane lipid rafts is necessary for the ordered assembly and release of infectious newcastle disease virus particles. J. Virol., November 1, 2006; 80(21): 10652 - 10662. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. G. P. Oomens, K. P. Bevis, and G. W. Wertz The Cytoplasmic Tail of the Human Respiratory Syncytial Virus F Protein Plays Critical Roles in Cellular Localization of the F Protein and Infectious Progeny Production J. Virol., November 1, 2006; 80(21): 10465 - 10477. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. W. McL. Rixon, G. Brown, J. T. Murray, and R. J. Sugrue The respiratory syncytial virus small hydrophobic protein is phosphorylated via a mitogen-activated protein kinase p38-dependent tyrosine kinase activity during virus infection J. Gen. Virol., February 1, 2005; 86(2): 375 - 384. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. C. Thorpe and A. J. Easton Genome sequence of the non-pathogenic strain 15 of pneumonia virus of mice and comparison with the genome of the pathogenic strain J3666 J. Gen. Virol., January 1, 2005; 86(1): 159 - 169. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |
