The carboxyl segment of the mumps virus V protein associates with Stat proteins in vitro via a tryptophan-rich motif

Article Article scientifique Article The carboxyl segment of the mumps virus V protein associates with Stat proteins in vitro via a tryptophan-rich motif eng 2002 author Nishio Machiko 133678 author Garcin Dominique 24296 author Simonet Viviane 88653 author Kolakofsky Daniel 25420 92-99 10.1006/viro.2002.1509 12202209 0042-6822 Viruses of the Paramyxovirinae, similar to other viruses, have evolved specific proteins that interdict IFN action as part of a general strategy to counteract host innate immunity. In many (but not all) cases, this interdiction is accompanied by a lowering of the intracellular levels of the STAT proteins. Among rubulaviruses, there is a notable variation in how they interfere with IFN action. Whereas SV41, SV5, and MuV all act by lowering Stat1, hPIV2 acts by lowering Stat2. Here, we show that the mumps and hPIV2 V proteins both form a complex with several Stat proteins in a mixed-extract assay. This suggests that the specific degradation of these Stat proteins is not determined by complex formation, but presumably at some later stage of the degradation pathway. V/Stat complex formation requires a specific carboxyl segment of V. However, a previously unrecognized trp-rich motif, rather than the Zn(++)-binding cys-cluster of this segment, appears to be required for V/Stat interaction. The C protein of Sendai (respiro-) virus, another P gene encoded protein, also forms a complex with Stat1, and prebinding of MuV V to Stat1 prevents the subsequent binding of SeV C. Our results suggest that rubulavirus V proteins may be related to both the C and the V proteins of respiroviruses. Animals Binding Sites Cells, Cultured DNA-Binding Proteins/metabolism Fibroblasts Mice Mumps virus/physiology Peptide Fragments/chemistry/metabolism Viral Proteins/chemistry/metabolism Dewey 616 54 Département de microbiologie et médecine moléculaire 21B false 216 Virologie moléculaire 275 Virology 300 1 72c78a0c-bf5e-4578-8f4b-45ad449c266b Article (Published version) Public 1-s2.0-S0042682202915096-main.pdf 267667 application/pdf openAccess Faculté de médecine / Section de médecine fondamentale / Département de microbiologie et médecine moléculaire

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The carboxyl segment of the mumps virus V protein associates with Stat proteins in vitro via a tryptophan-rich motif	Virology			2002	666	694

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Simonet, Viviane