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Proteomics Weekly


New research on respiratory syncytial virus from Monash University summarized



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This article was published in Proteomics Weekly, which you can subscribe to online.

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2009 JUL 13 - (NewsRx.com) -- According to recent research published in the Journal of Virology, "The respiratory syncytial virus (RSV) matrix ( M) protein is localized in the nucleus of infected cells early in infection but is mostly cytoplasmic late in infection. We have previously shown that M localizes in the nucleus through the action of the importin beta 1 nuclear import receptor."

"Here, we establish for the first time that M's ability to shuttle to the cytoplasm is due to the action of the nuclear export receptor Crm1, as shown in infected cells, and in cells transfected to express green fluorescent protein (GFP)-M fusion proteins. Specific inhibition of Crm1-mediated nuclear export by leptomycin B increased M nuclear accumulation. Analysis of truncated and point-mutated M derivatives indicated that Crm1-dependent nuclear export of M is attributable to a nuclear export signal (NES) within residues 194 to 206. Importantly, inhibition of M nuclear export resulted in reduced virus production, and a recombinant RSV carrying a mutated NES could not be rescued by reverse genetics. That this is likely to be due to the inability of a nuclear export deficient M to localize to regions of virus assembly is indicated by the fact that a nuclear-export-deficient GFP-M fails to localize to regions of virus assembly when expressed in cells infected with wild-type RSV," wrote R. Ghildyal and colleagues, Monash University.

The researchers concluded: "Together, our data suggest that Crm1-dependent nuclear export of M is central to RSV infection, representing the first report of such a mechanism for a paramyxovirus M protein and with important implications for related paramyxoviruses."

Ghildyal and colleagues published their study in the Journal of Virology (The Respiratory Syncytial Virus Matrix Protein Possesses a Crm1-Mediated Nuclear Export Mechanism. Journal of Virology, 2009;83(11):5353-5362).

For additional information, contact D.A. Jans, Monash University, Dept. of Biochemistry & Molecular Biology, Wellington Rd., Clayton, Vic 3800, Australia.

The publisher's contact information for the Journal of Virology is: American Society Microbiology, 1752 N St. NW, Washington, DC 20036-2904, USA.

Keywords: Australia, Clayton, Infectious Disease, Proteomics. Fusion Proteins, Pulmonology, Respiratory Syncytial Virus, Virology, Monash University.

This article was prepared by Proteomics Weekly editors from staff and other reports. Copyright 2009, Proteomics Weekly via NewsRx.com.

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