| Virus Name | Tick-borne encephalitis virus |
| Virus Short Name | TBEV |
| Order | Unassigned |
| Virus Family | Flaviviridae |
| Virus Subfamily | N.A. |
| Genus | Flavivirus |
| Species | Tick-borne encephalitis virus |
| Host | Human, mammals, mosquitoes and ticks |
| Cell Tropism | N.A. |
| Associated Disease | Meningitis and encephalitis |
| Mode of Transmission | Tick bite,from an infected mother to fetus |
| VIPR DB link | http://www.viprbrc.org/brc/home.spg?decorator=flavi |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_online_report/positive-sense-rna-viruses/w/flaviviridae |
| Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Flaviviridae |
| Paper Title | Identification and analysis of host proteins that interact with the 3?- untranslated region of tick-borne encephalitis virus genomic RNA |
| Author's Name | Memi Mutoa, Wataru Kamitanib, Mizuki Sakaia, Minato Hiranoa, Shintaro Kobayashia, Hiroaki Kariwaa, Kentaro Yoshii |
| Journal Name | Virus Research |
| Pubmed ID | 29545014 |
| Abstract | Tick-borne encephalitis virus (TBEV) causes severe neurological disease, but the pathogenetic mechanism is unclear. The conformational structure of the 3-untranslated region (UTR) of TBEV is associated with its virulence. We tried to identify host proteins interacting with the 3-UTR of TBEV. Cellular proteins of HEK293T cells were co-precipitated with biotinylated RNAs of the 3-UTR of low- and high-virulence TBEV strains and subjected to mass spectrometry analysis. Fifteen host proteins were found to bind to the 3-UTR of TBEV, four of which-cold shock domain containing-E1 (CSDE1), spermatid perinuclear RNA binding protein (STRBP), fragile X mental retardation protein (FMRP), and interleukin enhancer binding factor 3 (ILF3)-bound specifically to that of the low-virulence strain. An RNA immunoprecipitation and pull-down assay confirmed the interactions of the complete 3-UTRs of TBEV genomic RNA with CSDE1, FMRP, and ILF3. Partial deletion of the stem loop (SL) 3 to SL 5 structure of the variable region of the 3-UTR did not affect interactions with the host proteins, but the interactions were markedly suppressed by deletion of the complete SL 3, 4, and 5 structures, as in the high-virulence TBEV strain. Further analysis of the roles of host proteins in the neurologic pathogenicity of TBEV is warranted. |
| Used Model | HEK293T cells |
| DOI | 10.1016/j.virusres.2018.03.006 |
