| Virus Name | Measles Virus |
| Virus Short Name | MeV |
| Order | Mononegavirales |
| Virus Family | Paramyxoviridae |
| Virus Subfamily | N.A. |
| Genus | Morbilivirus |
| Species | Measles morbillivirus |
| Host | Vertebrates |
| Cell Tropism | N.A. |
| Associated Disease | Fever, rash |
| Mode of Transmission | Sexual contact, blood, breast feeding |
| VIPR DB link | http://www.viprbrc.org/brc/vipr_allSpecies_search.do?method=SubmitForm&decorator=paramyxo |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/negative-sense-rna-viruses-2011/w/negrna_viruses/199/paramyxoviridae |
| Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Paramyxoviridae |
| Paper Title | The measles virus phosphoprotein interacts with the linker domain of STAT1 |
| Author's Name | Patricia Devaux, Lauren Priniski and Roberto Cattaneo |
| Journal Name | Virology |
| Pubmed ID | 23856440 |
| Abstract | The measles virus (MV) phosphoprotein (P) and V proteins block the interferon (IFN) response by impeding phosphorylation of the signal transducer and activator of transcription 1 (STAT1) by the Janus kinase 1 (JAK1). We characterized how STAT1 mutants interact with P and JAK1 phosphorylation. Certain mutants of the linker, the Src-homology 2 domain (SH2), or the transactivation domain had reduced or abolished phosphorylation through JAK1 after IFN treatment. Other mutants, mainly localized in the linker, failed to interact with P as documented by the lack of interference with nuclear translocation. Thus the functional footprint of P on STAT1 localizes mainly to the linker domain; there is also some overlap with the STAT1 phosphorylation functional footprint on the SH2 domain. Based on these observations, we discuss how the MV-P might operate to inhibit the JAK/STAT pathway. |
| Used Model | U3A cells |
| DOI | 10.1016/j.virol.2013.06.019 |