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Title: Evidence that the respiratory syncytial virus polymerase complex associates with lipid rafts in virus-infected cells: a proteomic analysis

Abstract

The interaction between the respiratory syncytial virus (RSV) polymerase complex and lipid rafts was examined in HEp2 cells. Lipid-raft membranes were prepared from virus-infected cells and their protein content was analysed by Western blotting and mass spectrometry. This analysis revealed the presence of the N, P, L, M2-1 and M proteins. However, these proteins appeared to differ from one another in their association with these structures, with the M2-1 protein showing a greater partitioning into raft membranes compared to that of the N, P or M proteins. Determination of the polymerase activity profile of the gradient fractions revealed that 95% of the detectable viral enzyme activity was associated with lipid-raft membranes. Furthermore, analysis of virus-infected cells by confocal microscopy suggested an association between these proteins and the raft-lipid, GM1. Together, these results provide evidence that the RSV polymerase complex is able to associate with lipid rafts in virus-infected cells.

Authors:
 [1];  [2];  [1];  [1];  [3]
  1. MRC Virology Unit, Institute of Virology, Glasgow G11 5JR (United Kingdom)
  2. Sir Henry Wellcome Functional Genomics Facility, University of Glasgow, Glasgow, G12 8QQ (United Kingdom)
  3. MRC Virology Unit, Institute of Virology, Glasgow G11 5JR (United Kingdom). E-mail: r.sugrue@vir.gla.ac.uk
Publication Date:
OSTI Identifier:
20637182
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 330; Journal Issue: 1; Other Information: DOI: 10.1016/j.virol.2004.09.034; PII: S0042-6822(04)00648-8; Copyright (c) 2004 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ENZYME ACTIVITY; INTERACTIONS; LIPIDS; MASS SPECTROSCOPY; MEMBRANES; MICROSCOPY; PROTEINS; VIRUSES

Citation Formats

McDonald, Terence P., Pitt, Andrew R., Brown, Gaie, Rixon, Helen W. McL., and Sugrue, Richard J. Evidence that the respiratory syncytial virus polymerase complex associates with lipid rafts in virus-infected cells: a proteomic analysis. United States: N. p., 2004. Web. doi:10.1016/j.virol.2004.09.034.
McDonald, Terence P., Pitt, Andrew R., Brown, Gaie, Rixon, Helen W. McL., & Sugrue, Richard J. Evidence that the respiratory syncytial virus polymerase complex associates with lipid rafts in virus-infected cells: a proteomic analysis. United States. doi:10.1016/j.virol.2004.09.034.
McDonald, Terence P., Pitt, Andrew R., Brown, Gaie, Rixon, Helen W. McL., and Sugrue, Richard J. Sun . "Evidence that the respiratory syncytial virus polymerase complex associates with lipid rafts in virus-infected cells: a proteomic analysis". United States. doi:10.1016/j.virol.2004.09.034.
@article{osti_20637182,
title = {Evidence that the respiratory syncytial virus polymerase complex associates with lipid rafts in virus-infected cells: a proteomic analysis},
author = {McDonald, Terence P. and Pitt, Andrew R. and Brown, Gaie and Rixon, Helen W. McL. and Sugrue, Richard J.},
abstractNote = {The interaction between the respiratory syncytial virus (RSV) polymerase complex and lipid rafts was examined in HEp2 cells. Lipid-raft membranes were prepared from virus-infected cells and their protein content was analysed by Western blotting and mass spectrometry. This analysis revealed the presence of the N, P, L, M2-1 and M proteins. However, these proteins appeared to differ from one another in their association with these structures, with the M2-1 protein showing a greater partitioning into raft membranes compared to that of the N, P or M proteins. Determination of the polymerase activity profile of the gradient fractions revealed that 95% of the detectable viral enzyme activity was associated with lipid-raft membranes. Furthermore, analysis of virus-infected cells by confocal microscopy suggested an association between these proteins and the raft-lipid, GM1. Together, these results provide evidence that the RSV polymerase complex is able to associate with lipid rafts in virus-infected cells.},
doi = {10.1016/j.virol.2004.09.034},
journal = {Virology},
number = 1,
volume = 330,
place = {United States},
year = {Sun Dec 05 00:00:00 EST 2004},
month = {Sun Dec 05 00:00:00 EST 2004}
}