Virus Details


VHFID6672

Host Factor Information

Gene Name Eif3e
HF Protein Name Eukaryotic translation initiation factor 3 subunit E
HF Function Essential for viral translation
Uniprot ID P60229
Protein Sequence View Fasta Sequence
NCBI Gene ID 16341
Host Factor (HF) Name in Paper eIF3e
Gene synonyms Eif3s6 Int6
Ensemble Gene ID ENSMUSG00000022336
Ensemble Transcript ENSMUST00000022960
KEGG ID Go to KEGG Database
Gene Ontology ID(s) GO:0000184, GO:0003743, GO:0005634, GO:0005737, GO:0005829, GO:0005852, GO:0006413, GO:0016604, GO:0016605, GO:0045296, GO:0045727, GO:0047485, GO:1902416,
MINT ID P60229
STRING Click to see interaction map
GWAS Analysis Click to see gwas analysis
OMIM ID N.A.
PANTHER ID PTHR10317
PDB ID(s) N.A.,
pfam ID PF09440, PF01399,
Drug Bank ID N.A.,
ChEMBL ID N.A.
Organism Mus musculus (Mouse)

Pathogen Information

Virus Name Mouse mammary tumor virus
Virus Short Name MMTV
Order Unassigned
Virus Family Retroviridae
Virus Subfamily Orthoretrovirinae
Genus Gammaretrovirus
Species Mouse mammary tumor virus
Host Vertebrates
Cell Tropism T and B cells located in Peyer?s patches of the gastrointestinal tracts of neonatally infected pups
Associated Disease N.A.
Mode of Transmission N.A.
VIPR DB link N.A.
ICTV DB link https://talk.ictvonline.org/ictv-reports/ictv_9th_report/reverse-transcribing-dna-and-rna-viruses-2011/w/rt_viruses/161/retroviridae
Virus Host DB link http://www.genome.jp/virushostdb/view/?virus_lineage=Retroviridae

Publication Information

Paper Title Expression of truncated eukaryotic initiation factor 3e (eIF3e) resulting from integration of mouse mammary tumor virus (MMTV) causes a shift from cap-dependent to Cap-independent translation
Author's Name David Chiluiza, Sharon Bargo, Robert Callahan and Robert E. Rhoads
Journal Name Journal Of Biological Chemistry
Pubmed ID 21737453
Abstract Integration of mouse mammary tumor virus (MMTV) at the common integration site Int6 occurs in the gene encoding eIF3e, the p48 subunit of translation initiation factor eIF3. Integration is at any of several introns of the Eif3e gene and causes the expression of truncated Eif3e mRNAs. Ectopic expression of the truncated eIF3e protein resulting from integration at intron 5 (3e5) induces malignant transformation, but by an unknown mechanism. Because eIF3e makes up at least part of the binding site for eIF4G, we examined the effects of 3e5 expression on protein synthesis. We developed an NIH3T3 cell line that contains a single copy of the 3e5 sequence at a predetermined genomic site. Co-immunoprecipitation indicated diminished binding of eIF3 to eIF4G, signifying a reduction in recruitment of the mRNA-unwinding machinery to the 43 S preinitiation complex. Cell growth and overall protein synthesis were decreased. Translation driven by the eIF4G-independent hepatitis C virus internal ribosome entry sequence (HCV IRES) in a bicistronic mRNA was increased relative to cap-dependent translation. Endogenous mRNAs encoding XIAP, c-Myc, CYR61, and Pim-1, which are translated in a cap-independent manner, were shifted to heavier polysomes whereas mRNAs encoding GAPDH, actin, L32, and L34, which are translated in a cap-dependent manner, were shifted to lighter polysomes. We propose that expression of 3e5 diminishes eIF4G interaction with eIF3 and causes abnormal gene expression at the translational level. The correlation between up-regulation of cap-independent translation and MMTV-induced tumorigenesis contrasts with the well established model for malignant transformation involving up-regulation of highly cap-dependent translation.
Used Model NIH3T3 cells
DOI 10.1074/jbc.M111.267294