A point mutation, E95D, in the mumps virus V protein disengages STAT3 targeting from STAT1 targeting

Mamta Puri, Ken Lemon, W. Paul Duprex, Bertus K. Rima, Curt M. Horvath

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)6347-6356
Number of pages10
JournalJournal of virology
Issue number13
StatePublished - Jul 2009

ASJC Scopus subject areas

  • Insect Science
  • Virology
  • Microbiology
  • Immunology


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