Escaping from the cell: assembly and budding of negative-strand RNA viruses

Curr Top Microbiol Immunol. 2004;283:145-96. doi: 10.1007/978-3-662-06099-5_5.

Abstract

Negative-strand RNA virus particles are formed by a process that includes the assembly of viral components at the plasma membranes of infected cells and the subsequent release of particles by budding. Here, we review recent progress that has been made in understanding the mechanisms of negative-strand RNA virus assembly and bud- ding. Important topics for discussion include the key role played by the viral matrix proteins in assembly of viruses and viruslike particles, as well as roles played by additional viral components such as the viral glycoproteins. Various interactions that contribute to virus assembly are discussed, including interactions between matrix proteins and membranes, interactions between matrix proteins and glycoproteins, interactions between matrix proteins and nucleocapsids, and interactions that lead to matrix protein self-assembly. Selection of specific sites on plasma membranes to be used for virus assembly and budding is described, including the asymmetric budding of some viruses in polarized epithelial cells and assembly of viral components in lipid raft microdomains. Evidence for the involvement of cellular proteins in the late stages of rhabdovirus and filovirus budding is discussed as well as the possible involvement of similar host factors in the late stages of budding of other negative-strand RNA viruses.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Cell Membrane / virology
  • Eukaryotic Cells / virology
  • HN Protein / metabolism
  • HN Protein / physiology
  • Membrane Microdomains / metabolism
  • Membrane Microdomains / virology
  • Nucleocapsid / metabolism
  • RNA Viruses / chemistry
  • RNA Viruses / physiology*
  • Viral Matrix Proteins / metabolism
  • Viral Matrix Proteins / physiology
  • Virus Assembly*

Substances

  • HN Protein
  • Viral Matrix Proteins