| Gene Name | EIF3L |
| HF Protein Name | Eukaryotic translation initiation factor 3 subunit L |
| HF Function | Essential for virus replication |
| Uniprot ID | Q9Y262 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 51386 |
| Host Factor (HF) Name in Paper | EIF3L |
| Gene synonyms | EIF3EIP EIF3S6IP |
| Ensemble Gene ID | ENSG00000100129 |
| Ensemble Transcript | ENST00000381683 [Q9Y262-2];ENST00000624234 [Q9Y262-1] |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0001650, GO:0003723, GO:0003743, GO:0005654, GO:0005829, GO:0005852, GO:0006413, GO:0016020, GO:0075525, |
| MINT ID | Q9Y262 |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | N.A. |
| PANTHER ID | PTHR13242 |
| PDB ID(s) | 3J8B, 3J8C, 6FEC, |
| pfam ID | PF10255, |
| Drug Bank ID | N.A., |
| ChEMBL ID | N.A. |
| Organism | Homo sapiens (Human) |
| Virus Name | Yellow fever virus |
| Virus Short Name | YFV |
| Order | Unassigned |
| Virus Family | Flaviviridae |
| Virus Subfamily | N.A. |
| Genus | Flavivirus |
| Species | Yellow fever virus |
| Host | Human, mammals, mosquitoes and ticks |
| Cell Tropism | N.A. |
| Associated Disease | Hemorrhagic fever, encephalitis |
| Mode of Transmission | Arthropod bite, mainly mosquitoes |
| VIPR DB link | http://www.viprbrc.org/brc/home.spg?decorator=flavi |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_online_report/positive-sense-rna-viruses/w/flaviviridae |
| Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Flaviviridae |
| Paper Title | The eukaryotic translation initiation factor 3 subunit L protein interacts with Flavivirus NS5 and may modulate yellow fever virus replication |
| Author's Name | Ana TS Morais, Ana CB Terzian, Danilo VB Duarte, Roberta VM Bronzoni, Maria CFS Madrid, Arieli F Gavioli, Laura HVG Gil, Amanda G Oliveira, Cleslei F Zanelli, Sandro R Valentini, Paula Rahal and Mauricio L Nogueira |
| Journal Name | Virology Journal |
| Pubmed ID | 23800076 |
| Abstract | BACKGROUND: Yellow fever virus (YFV) belongs to the Flavivirus genus and causes an important disease. An alarming resurgence of viral circulation and the expansion of YFV-endemic zones have been detected in Africa and South America in recent years. NS5 is a viral protein that contains methyltransferase and RNA-dependent RNA polymerase (RdRp) domains, which are essential for viral replication, and the interactions between NS5 and cellular proteins have been studied to better understand viral replication. The aim of this study was to characterize the interaction of the NS5 protein with eukaryotic translation initiation factor 3 subunit L (eIF3L) and to evaluate the role of eIF3L in yellow fever replication. METHODS: To identify interactions of YFV NS5 with cellular proteins, we performed a two-hybrid screen using the YFV NS5 RdRp domain as bait with a human cDNA library, and RNApol deletion mutants were generated and analyzed using the two-hybrid system for mapping the interactions. The RNApol region involved was segmented into three fragments and analyzed using an eIF3L-expressing yeast strain. To map the NS5 residues that are critical for the interactions, we performed site-direct mutagenesis in segment 3 of the interaction domain (ID) and confirmed the interaction using in vitro assays and in vivo coimmunoprecipitation. The significance of eIF3L for YFV replication was investigated using eIF3L overexpression and RNA interference. RESULTS: In this work, we describe and characterize the interaction of NS5 with the translation factor eIF3L. The interaction between NS5 and eIF3L was confirmed using in vitro binding and in vivo coimmunoprecipitation assays. This interaction occurs at a region (the interaction domain of the RNApol domain) that is conserved in several flaviviruses and that is, therefore, likely to be relevant to the genus. eIF3L overexpression and plaque reduction assays showed a slight effect on YFV replication, indicating that the interaction of eIF3L with YFV NS5 may play a role in YFV replication. CONCLUSIONS: Although the precise function of eIF3L on interactions with viral proteins is not entirely understood, these results indicate an interaction of eIF3L with YF NS5 and that eIF3L overexpression facilitates translation, which has potential implications for virus replication. |
| Used Model | HeLa cells |
| DOI | 10.1186/1743-422X-10-205 |
