Gene Name | IFIT1 |
HF Protein Name | Interferon-induced protein with tetratricopeptide repeats 1 |
HF Function | Inhibits mRNA translation of Rubulaviruses |
Uniprot ID | P09914 |
Protein Sequence | View Fasta Sequence |
NCBI Gene ID | 3434 |
Host Factor (HF) Name in Paper | IFIT1 |
Gene synonyms | G10P1 IFI56 IFNAI1 ISG56 |
Ensemble Gene ID | ENSG00000185745 |
Ensemble Transcript | ENST00000371804 [P09914-1];ENST00000546318 [P09914-2] |
KEGG ID | Go to KEGG Database |
Gene Ontology ID(s) | GO:0003723, GO:0005737, GO:0005829, GO:0009615, GO:0016032, GO:0019060, GO:0032091, GO:0043657, GO:0045070, GO:0045071, GO:0050689, GO:0051097, GO:0051607, GO:0060337, GO:0071357, GO:0071360, |
MINT ID | P09914 |
STRING | Click to see interaction map |
GWAS Analysis | Click to see gwas analysis |
OMIM ID | 147690 |
PANTHER ID | PTHR10271:SF22 |
PDB ID(s) | 4HOU, 5UDI, 5UDJ, 5UDK, 5UDL, 5W5H, 5W5I, |
pfam ID | PF13181, |
Drug Bank ID | N.A., |
ChEMBL ID | N.A. |
Organism | Homo sapiens (Human) |
Virus Name | Mumps virus |
Virus Short Name | MuV |
Order | Mononegavirales |
Virus Family | Paramyxoviridae |
Virus Subfamily | N.A. |
Genus | Rubulavirus |
Species | Mumps rubulavirus |
Host | Humans, apes, pigs, dogs |
Cell Tropism | N.A. |
Associated Disease | Mumps |
Mode of Transmission | Respiratory, saliva |
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 | Human IFIT1 inhibits mRNA translation of rubulaviruses but Not Other members of the paramyxoviridae family |
Author's Name | D. F. Young, J. Andrejeva, X. Li, F. Inesta-Vaquera, C. Dong, V. H. Cowling, S. Goodbourn, R. E. Randall |
Journal Name | Journal Of Virology |
Pubmed ID | 27512068 |
Abstract | We have previously shown that IFIT1 is primarily responsible for the antiviral action of interferon (IFN) alpha/beta against parainfluenza virus type 5 (PIV5), selectively inhibiting the translation of PIV5 mRNAs. Here we report that while PIV2, PIV5, and mumps virus (MuV) are sensitive to IFIT1, nonrubulavirus members of the paramyxoviridae such as PIV3, Sendai virus (SeV), and canine distemper virus (CDV) are resistant. The IFIT1 sensitivity of PIV5 was not rescued by coinfection with an IFIT1-resistant virus (PIV3), demonstrating that PIV3 does not specifically inhibit the antiviral activity of IFIT1 and that the inhibition of PIV5 mRNAs is regulated by cis-acting elements. We developed an in vitro translation system using purified human IFIT1 to further investigate the mechanism of action of IFIT1. While the translations of PIV2, PIV5, and MuV mRNAs were directly inhibited by IFIT1, the translations of PIV3, SeV, and CDV mRNAs were not. Using purified human mRNA-capping enzymes, we show biochemically that efficient inhibition by IFIT1 is dependent upon a 5 guanosine nucleoside cap (which need not be N7 methylated) and that this sensitivity is partly abrogated by 2O methylation of the cap 1 ribose. Intriguingly, PIV5 M mRNA, in contrast to NP mRNA, remained sensitive to inhibition by IFIT1 following in vitro 2O methylation, suggesting that other structural features of mRNAs may influence their sensitivity to IFIT1. Thus, surprisingly, the viral polymerases (which have 2-O-methyltransferase activity) of rubulaviruses do not protect these viruses from inhibition by IFIT1. Possible biological consequences of this are discussed. |
Used Model | A549 cells |
DOI | 10.1128/JVI.01056-16 |