Virus Name | Measles Virus |
Virus Short Name | MeV |
Order | Mononegavirales |
Virus Family | Paramyxoviridae |
Virus Subfamily | N.A. |
Genus | Morbilivirus |
Species | Measles morbillivirus |
Host | Human, dog, cattle |
Cell Tropism | N.A. |
Associated Disease | Fever, rash |
Mode of Transmission | Respiratory |
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 |