Virus Details


VHFID6675

Host Factor Information

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)

Pathogen Information

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

Publication Information

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