2009/04/23 by Mamta Puri, Ken Lemon, W. Paul Duprex +2 · 1 citation
Biochemistry, Genetics and Molecular Biology · Medicine · #Biology #Cancer research #Cell biology #Gene #Genetics #Molecular biology #Mumps virus #Mutation #Point mutation #STAT1 #STAT3 #Signal transduction #Virology #Virology and Viral Diseases #Virus #Virus-based gene therapy research #vaccines and immunoinformatics approaches
paper · doi:10.1128/jvi.00596-09
openalex publication_date 2009/04/23 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
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.