Sorting of the Respiratory Syncytial Virus Matrix Protein Into Detergent-Resistant Structures Is Dependent on Cell-Surface Expression of the Glycoproteins

Virology. 2002 Sep 1;300(2):244-54. doi: 10.1006/viro.2002.1540.

Abstract

The interaction of the respiratory syncytial virus (RSV) Matrix (M) protein with the plasma membrane was investigated using polyclonal and monoclonal antisera raised against recombinant M expressed in bacteria. M bound mainly to the plasma membrane, although a significant proportion bound to internal membranes. However, no localisation of M with the Golgi was observed, suggesting that transport of M to the plasma membrane was independent of the transport mechanism for the viral glycoproteins. Expression from a recombinant baculovirus demonstrated the ability of M to bind membranes in the absence of viral glycoprotein expression. When cell-surface expression of the viral glycoproteins was prevented using Brefeldin A, M was still found in association with the plasma membrane, but the characteristics of M's membrane-binding ability were different to that found in untreated infected cells. In the presence of normal glycoprotein expression, M was sorted into lipid rafts and, in addition, formed structures that could only be disrupted by treatment with high salt buffers, a feature suggesting an interaction with the cytoskeleton or the formation of strong intramolecular associations. Brefeldin A prevented M from being sorted into lipid rafts or from forming strong intramolecular associations. Brefeldin A also affected the stability of M bound to the plasma membrane, as M was more readily dissociated in the presence of the inhibitor. Coexpression of M and F resulted in the incorporation of M into lipid rafts but did not cause the formation of the strong intramolecular bonds, suggesting that additional factors are required for this phenomena.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brefeldin A / pharmacology
  • Cell Membrane / metabolism*
  • Detergents / pharmacology
  • Humans
  • Membrane Glycoproteins / physiology*
  • Membrane Microdomains / chemistry
  • Mice
  • Mice, Inbred BALB C
  • Viral Envelope Proteins / physiology*
  • Viral Matrix Proteins / analysis
  • Viral Matrix Proteins / chemistry*
  • Viral Matrix Proteins / metabolism
  • Viral Proteins / analysis
  • Viral Proteins / chemistry*
  • Viral Proteins / metabolism

Substances

  • Detergents
  • Membrane Glycoproteins
  • Viral Envelope Proteins
  • Viral Matrix Proteins
  • Viral Proteins
  • Brefeldin A