| Gene Name | EIF4G1 |
| HF Protein Name | Eukaryotic translation initiation factor 4 gamma 1 |
| HF Function | Essential for virus replication |
| Uniprot ID | Q04637 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 1981 |
| Host Factor (HF) Name in Paper | EIF4G |
| Gene synonyms | EIF4F EIF4G EIF4GI |
| Ensemble Gene ID | ENSG00000106263 |
| Ensemble Transcript | ENST00000342981 [Q04637-8];ENST00000346169 [Q04637-1];ENST00000350481 [Q04637-5];ENST00000352767 [Q04637-9];ENST00000382330 [Q04637-9];ENST00000392537 [Q04637-4];ENST00000414031 [Q04637-3];ENST00000424196 [Q04637-9];ENST00000434061 [Q04637-7];ENST00000435046 [Q04637-6] |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0000184, GO:0000289, GO:0001662, GO:0002191, GO:0003723, GO:0003729, GO:0003743, GO:0005524, GO:0005634, GO:0005737, GO:0005829, GO:0005844, GO:0006412, GO:0006413, GO:0006446, GO:0007005, GO:0008135, GO:0008190, GO:0008284, GO:0010507, GO:0010801, GO:0010942, GO:0016020, GO:0016032, GO:0016281, GO:0030307, GO:0031369, GO:0031669, GO:0032270, GO:0032502, GO:0032947, GO:0033138, GO:0034645, GO:0042802, GO:0043488, GO:0045296, GO:0045666, GO:0060964, GO:0080135, GO:0097009, GO:1900087, GO:1901215, GO:1905537, GO:1905606, GO:1905612, GO:1905618, GO:1905696, |
| MINT ID | Q04637 |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | 600495 |
| PANTHER ID | PTHR23253:SF10 |
| PDB ID(s) | 1LJ2, 1UG3, 2W97, 4AZA, 4F02, 5EHC, 5EI3, 5EIR, 5T46, |
| pfam ID | PF02847, PF02854, PF02020, |
| Drug Bank ID | N.A., |
| ChEMBL ID | N.A. |
| Organism | Homo sapiens (Human) |
| Virus Name | Coxsackievirus B3 |
| Virus Short Name | CV-B3 |
| Order | Picornavirales |
| Virus Family | Picornaviridae |
| Virus Subfamily | N.A. |
| Genus | Enterovirus |
| Species | Enterovirus B |
| Host | Human, mammals |
| Cell Tropism | The gastrointestinal trac |
| Associated Disease | Coxsackievirus-induced cardiomyopathy |
| Mode of Transmission | Either fecal-oral or respiratory |
| VIPR DB link | https://www.viprbrc.org/brc/home.spg?decorator=picorna |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/positive-sense-rna-viruses-2011/w/posrna_viruses/234/picornaviridae |
| Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Picornaviridae |
| Paper Title | Impaired binding of standard initiation factors eIF3b, eIF4G and eIF4B to domain V of the live-attenuated coxsackievirus B3 Sabin3-like IRES - alternatives for 5?UTR-related cardiovirulence mechanisms |
| Author's Name | Amira Souii, Jawhar Gharbi and Manel Ben Mhadheb-Gharbi |
| Journal Name | Diagnostic Pathology |
| Pubmed ID | 24063684 |
| Abstract | Internal ribosome entry site (IRES) elements fold into highly organized conserved secondary and probably tertiary structures that guide the ribosome to an internal site of the RNA at the IRES 3end. The composition of the cellular proteome is under the control of multiple processes, one of the most important being translation initiation. In each poliovirus Sabin vaccine strain, a single point mutation in the IRES secondary-structure domain V is a major determinant of neurovirulence and translation attenuation. Here we are extrapolating poliovirus findings to a genomic related virus named coxsackievirus B3 CVB3) a causative agent of viral myocarditis. We have previously reported that Sabin3-like mutation (U473 → C) introduced in the domain V sequence of the CVB3 IRES led to a defective mutant with a serious reduction in translation efficiency and ribosomal initiation complex assembly, besides an impaired RNA-protein binding pattern. With the aim to identify proteins interacting with both CVB3 wild-type and Sabin3-like domain V RNAs and to assess the effect of the Sabin3-like mutation on these potential interactions, we have used a proteomic approach. This procedure allowed the identification of three RNA-binding proteins interacting with the domain V: eIF4G (p220), eIF3b (p116) and eIF4B (p80). Moreover, we report that this single-nucleotide exchange impairs the interaction pattern and the binding affinity of these standard translation initiationfactors within the IRES domain V of the mutant strain. Taken together, these data indicate how this decisive Sabin3-like mutation mediates viral translation attenuation playing a key role in the understanding of the cardiovirulence attenuation within this construct. Hence, these data provide further evidence for the crucial role of RNA structure for the IRES activity, and reinforce the idea of a distribution of function between the different IRES structural domains. |
| Used Model | HeLa and BHK-21 cells |
| DOI | 10.1186/1746-1596-8-161 |
