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

Published in Virology. 2002, vol. 300, no. 1, p. 92-9
Abstract 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.
Keywords AnimalsBinding SitesCells, CulturedDNA-Binding Proteins/metabolismFibroblastsMiceMumps virus/physiologyPeptide Fragments/chemistry/metabolismViral Proteins/chemistry/metabolism
PMID: 12202209
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Research group Virologie moléculaire (275)
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NISHIO, Machiko et al. The carboxyl segment of the mumps virus V protein associates with Stat proteins in vitro via a tryptophan-rich motif. In: Virology, 2002, vol. 300, n° 1, p. 92-9. doi: 10.1006/viro.2002.1509 https://archive-ouverte.unige.ch/unige:38134

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Deposited on : 2014-06-25

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