Measles virus nucleocapsid transport to the plasma membrane requires stable expression and surface accumulation of the viral matrix protein

Cell Microbiol. 2007 May;9(5):1203-14. doi: 10.1111/j.1462-5822.2006.00860.x. Epub 2007 Jan 9.


In measles virus (MV)-infected cells the matrix (M) protein plays a key role in virus assembly and budding processes at the plasma membrane because it mediates the contact between the viral surface glycoproteins and the nucleocapsids. By exchanging valine 101, a highly conserved residue among all paramyxoviral M proteins, we generated a recombinant MV (rMV) from cloned cDNA encoding for a M protein with an increased intracellular turnover. The mutant rMV was barely released from the infected cells. This assembly defect was not due to a defective M binding to other matrix- or nucleoproteins, but could rather be assigned to a reduced ability to associate with cellular membranes, and more importantly, to a defective accumulation at the plasma membrane which was accompanied by the deficient transport of nucleocapsids to the cell surface. Thus, we show for the first time that M stability and accumulation at intracellular membranes is a prerequisite for M and nucleocapsid co-transport to the plasma membrane and for subsequent virus assembly and budding processes.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Transport
  • Cell Membrane / metabolism*
  • Cell Membrane / virology
  • Cells, Cultured
  • Chlorocebus aethiops
  • HeLa Cells
  • Humans
  • Immunoprecipitation
  • Measles virus / genetics
  • Measles virus / growth & development
  • Measles virus / metabolism*
  • Microscopy, Confocal
  • Microscopy, Fluorescence
  • Mutagenesis, Site-Directed
  • Mutation
  • Nucleocapsid / metabolism*
  • Vero Cells
  • Viral Matrix Proteins / genetics
  • Viral Matrix Proteins / metabolism*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism
  • Virus Assembly / genetics
  • Virus Assembly / physiology


  • Viral Matrix Proteins
  • Viral Proteins