Virus Details


VHFID7480

Host Factor Information

Gene Name EIF4G2
HF Protein Name Eukaryotic translation initiation factor 4 gamma 2
HF Function Essential for viral DNA replication
Uniprot ID P78344
Protein Sequence View Fasta Sequence
NCBI Gene ID 1982
Host Factor (HF) Name in Paper eIF4GII
Gene synonyms DAP5
Ensemble Gene ID ENSG00000110321
Ensemble Transcript ENST00000640650 [P78344-1]
KEGG ID Go to KEGG Database
Gene Ontology ID(s) GO:0003723, GO:0003743, GO:0005829, GO:0005913, GO:0006446, GO:0007050, GO:0008135, GO:0008219, GO:0010507, GO:0016020, GO:0016281, GO:0030307, GO:0034645, GO:0045296,
MINT ID P78344
STRING Click to see interaction map
GWAS Analysis Click to see gwas analysis
OMIM ID 602325
PANTHER ID N.A.
PDB ID(s) 3D3M, 3L6A, 4IUL,
pfam ID PF02847, PF02854, PF02020,
Drug Bank ID N.A.,
ChEMBL ID N.A.
Organism Homo sapiens (Human)

Pathogen Information

Virus Name Vaccinia Virus
Virus Short Name VACV
Order Unassigned
Virus Family Poxviridae
Virus Subfamily Chordopoxvirinae
Genus Orthopoxvirus
Species Vaccinia virus
Host Human, mammals
Cell Tropism Dendritic cells, monocytes/macrophages, b lymphocytes, activated t lymphocytes
Associated Disease N.A.
Mode of Transmission N.A.
VIPR DB link https://www.viprbrc.org/brc/home.spg?decorator=pox
ICTV DB link https://talk.ictvonline.org/ictv-reports/ictv_9th_report/dsdna-viruses-2011/w/dsdna_viruses/74/poxviridae
Virus Host DB link http://www.genome.jp/virushostdb/view/?virus_lineage=Poxviridae

Publication Information

Paper Title Translation of mRNAs from vesicular stomatitis virus and vaccinia virus is differentially blocked in cells with depletion of eIF4GI and/or eIF4GII
Author's Name Ewelina Welnowska, Alfredo Castello, Pablo Moral and Luis Carrasco
Journal Name Journal Of Molecular Biology
Pubmed ID 19769989
Abstract Cytolytic viruses abrogate host protein synthesis to maximize the translation of their own mRNAs. In this study, we analyzed the eukaryotic initiation factor (eIF) 4G requirement for translation of vesicular stomatitis virus (VSV) and vaccinia virus (VV) mRNAs in HeLa cells using two different strategies: eIF4G depletion by small interfering RNAs or cleavage of eIF4G by expression of poliovirus 2A protease. Depletion of eIF4GI or eIF4GII moderately inhibits cellular protein synthesis, whereas silencing of both factors has only a slightly higher effect. Under these conditions, the extent of VSV protein synthesis is similar to that of nondepleted control cells, whereas VV expression is substantially reduced. Similar results were obtained when eIF4E was depleted. On the other hand, eIF4G cleavage by poliovirus 2A protease strongly inhibits translation of VV protein expression, whereas translation directed by VSV mRNAs is not abrogated, even though VSV mRNAs are capped. Therefore, the requirement for eIF4F activity is different for VV and VSV, suggesting that the molecular mechanism by which their mRNAs initiate their translation is also different. Consistent with these findings, eIF4GI does not colocalize with ribosomes in VSV-infected cells, while eIF2alpha locates at perinuclear sites coincident with ribosomes.
Used Model HeLa cells
DOI 10.1016/j.jmb.2009.09.036