Abstract:
:Mumps virus, like other paramyxoviruses in the Rubulavirus genus, encodes a V protein that can assemble a ubiquitin ligase complex from cellular components, leading to the destruction of cellular signal transducer and activator of transcription (STAT) proteins. While many V proteins target the interferon-activated STAT1 or STAT2 protein, mumps virus V protein is unique in its ability to also target STAT3 for ubiquitin modification and proteasome-mediated degradation. Here we report that a single amino acid substitution in the mumps virus V protein, E95D, results in defective STAT3 targeting while maintaining the ability to target STAT1. Results indicate that the E95D mutation disrupts the ability of the V protein to associate with STAT3. A recombinant mumps virus carrying the E95D mutation in its P and V proteins replicates normally in cultured cells but fails to induce targeting of STAT3. Infection with the recombinant virus results in the differential regulation of a number of cellular genes compared to wild-type mumps virus and increases cell death in infected cells, producing a large-plaque phenotype.
journal_name
J Viroljournal_title
Journal of virologyauthors
Puri M,Lemon K,Duprex WP,Rima BK,Horvath CMdoi
10.1128/JVI.00596-09subject
Has Abstractpub_date
2009-07-01 00:00:00pages
6347-56issue
13eissn
0022-538Xissn
1098-5514pii
JVI.00596-09journal_volume
83pub_type
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pub_type: 杂志文章
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更新日期:1999-11-01 00:00:00