Measles virus nucleocapsid transport to the plasma membrane requires stable expression and surface accumulation of the viral matrix protein
- PMID: 17217427
- DOI: 10.1111/j.1462-5822.2006.00860.x
Measles virus nucleocapsid transport to the plasma membrane requires stable expression and surface accumulation of the viral matrix protein
Abstract
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.
Similar articles
-
Inefficient measles virus budding in murine L.CD46 fibroblasts.Virology. 1999 Dec 20;265(2):185-95. doi: 10.1006/viro.1999.0064. Virology. 1999. PMID: 10600591
-
The assembly of the measles virus nucleoprotein into nucleocapsid-like particles is modulated by the phosphoprotein.Virology. 1997 Jun 9;232(2):260-8. doi: 10.1006/viro.1997.8568. Virology. 1997. PMID: 9191839
-
Assembly of nucleocapsids with cytosolic and membrane-derived matrix proteins of vesicular stomatitis virus.Virology. 1999 Sep 1;261(2):295-308. doi: 10.1006/viro.1999.9856. Virology. 1999. PMID: 10497115
-
Rhabdovirus assembly and budding.Virus Res. 2004 Dec;106(2):117-32. doi: 10.1016/j.virusres.2004.08.009. Virus Res. 2004. PMID: 15567492 Review.
-
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.
Cited by
-
Mutated Measles Virus Matrix and Fusion Protein Influence Viral Titer In Vitro and Neuro-Invasion in Lewis Rat Brain Slice Cultures.Viruses. 2021 Apr 1;13(4):605. doi: 10.3390/v13040605. Viruses. 2021. PMID: 33916225 Free PMC article.
-
The C-terminal end of parainfluenza virus 5 NP protein is important for virus-like particle production and M-NP protein interaction.J Virol. 2010 Dec;84(24):12810-23. doi: 10.1128/JVI.01885-10. Epub 2010 Oct 13. J Virol. 2010. PMID: 20943976 Free PMC article.
-
Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions.Proc Natl Acad Sci U S A. 2011 Nov 1;108(44):18085-90. doi: 10.1073/pnas.1105770108. Epub 2011 Oct 24. Proc Natl Acad Sci U S A. 2011. PMID: 22025713 Free PMC article.
-
Mutations in the Transmembrane Domain and Cytoplasmic Tail of Hendra Virus Fusion Protein Disrupt Virus-Like-Particle Assembly.J Virol. 2017 Jun 26;91(14):e00152-17. doi: 10.1128/JVI.00152-17. Print 2017 Jul 15. J Virol. 2017. PMID: 28468881 Free PMC article.
-
Emerging paramyxoviruses: molecular mechanisms and antiviral strategies.Expert Rev Mol Med. 2011 Feb 24;13:e6. doi: 10.1017/S1462399410001754. Expert Rev Mol Med. 2011. PMID: 21345285 Free PMC article. Review.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
