Escaping from the cell: assembly and budding of negative-strand RNA viruses
- PMID: 15298170
- DOI: 10.1007/978-3-662-06099-5_5
Escaping from the cell: assembly and budding of negative-strand RNA viruses
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.
Similar articles
-
Assembly and budding of influenza virus.Virus Res. 2004 Dec;106(2):147-65. doi: 10.1016/j.virusres.2004.08.012. Virus Res. 2004. PMID: 15567494 Free PMC article. Review.
-
Assembly and budding of negative-strand RNA viruses.Adv Virus Res. 2013;85:57-90. doi: 10.1016/B978-0-12-408116-1.00003-3. Adv Virus Res. 2013. PMID: 23439024 Review.
-
Influenza virus morphogenesis and budding.Virus Res. 2009 Aug;143(2):147-61. doi: 10.1016/j.virusres.2009.05.010. Epub 2009 May 27. Virus Res. 2009. PMID: 19481124 Free PMC article. Review.
-
Requirements for budding of paramyxovirus simian virus 5 virus-like particles.J Virol. 2002 Apr;76(8):3952-64. doi: 10.1128/jvi.76.8.3952-3964.2002. J Virol. 2002. PMID: 11907235 Free PMC article.
-
A role for caveolin 1 in assembly and budding of the paramyxovirus parainfluenza virus 5.J Virol. 2010 Oct;84(19):9749-59. doi: 10.1128/JVI.01079-10. Epub 2010 Jul 14. J Virol. 2010. PMID: 20631121 Free PMC article.
Cited by
-
Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state.J Virol. 2004 Dec;78(24):13727-42. doi: 10.1128/JVI.78.24.13727-13742.2004. J Virol. 2004. PMID: 15564482 Free PMC article.
-
Vaccine potential of Nipah virus-like particles.PLoS One. 2011 Apr 6;6(4):e18437. doi: 10.1371/journal.pone.0018437. PLoS One. 2011. PMID: 21494680 Free PMC article.
-
Role of the cytoplasmic tail domains of Bunyamwera orthobunyavirus glycoproteins Gn and Gc in virus assembly and morphogenesis.J Virol. 2007 Sep;81(18):10151-60. doi: 10.1128/JVI.00573-07. Epub 2007 Jul 3. J Virol. 2007. PMID: 17609275 Free PMC article.
-
Characterization of the Tupaia rhabdovirus genome reveals a long open reading frame overlapping with P and a novel gene encoding a small hydrophobic protein.J Virol. 2005 Jun;79(11):6781-90. doi: 10.1128/JVI.79.11.6781-6790.2005. J Virol. 2005. PMID: 15890917 Free PMC article.
-
Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus.J Mol Biol. 2004 Oct 29;343(4):819-31. doi: 10.1016/j.jmb.2004.08.071. J Mol Biol. 2004. PMID: 15476803 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources