Studies from M. Colombo and co-researchers yield new data on measles
2009 AUG 4 - (NewsRx.com) -- According to recent research from Lyon, France, "The genome of measles virus consists of a non-segmented single-stranded RNA molecule of negative polarity, which is encapsidated by the viral nucleoprotein (N) within a helical nucleocapsid. The N protein possesses an intrinsically disordered C-terminal domain (aa 401-525, N-TAIL) that is exposed at the surface of the viral nucleopcapsid." "Thanks to its flexible nature, NTAIL interacts with several viral and cellular partners. Among these latter, the Interferon Regulator Factor 3 (IRF-3) has been reported to interact with N, with the interaction having been mapped to the regulatory domain of IRF-3 and to NTAIL. This interaction was described to lead to the phosphorylation-dependent activation of IRF-3, and to the ensuing activation of the pro-immune cytokine RANTES gene. After confirming the reciprocal ability of IRF-3 and N to be co-immunoprecipitated in 293T cells, we thoroughly investigated the N-TAIL-IRF-3 interaction using a recombinant, monomeric form of the regulatory domain of IRF-3. Using a large panel of spectroscopic approaches, including circular dichroism, fluorescence spectroscopy, nuclear magnetic resonance and electron paramagnetic resonance spectroscopy, we failed to detect any direct interaction between IRF-3 and either full-length N or NTAIL under conditions where these latter interact with the C-terminal X domain of the viral phosphoprotein. Furthermore, such interaction was neither detected in E. coli nor in a yeast two hybrid assay. Altogether, these data support the requirement for a specific cellular environment, such as that provided by 293T human cells, for the NTAIL-IRF-3 interaction to occur," wrote M. Colombo and colleagues. The researchers concluded: "This dependence from a specific cellular context likely reflects the requirement for a human or mammalian cellular co-factor." Colombo and colleagues published their study in Virology Journal (The interaction between the measles virus nucleoprotein and the Interferon Regulator Factor 3 relies on a specific cellular environment. Virology Journal, 2009;6():59). For additional information, contact D. Gerlier, CNRS, FRE 3011, VirPatH, F-69372 Lyon, France. Publisher contact information for the Virology Journal is: Biomedical Central Ltd., Current Science Group, Middlesex House, 34-42 Cleveland St., London W1T 4LB, England. Keywords: France, Lyon, Interferon, Measles, Nucleocapsid, Viral Research, Virology. This article was prepared by Drug Law Weekly editors from staff and other reports. Copyright 2009, Drug Law Weekly via NewsRx.com.
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