| Virus Name | Swine flue virus |
| Virus Short Name | H1N1 |
| Order | Unassigned |
| Virus Family | Orthomyxoviridae |
| Virus Subfamily | N.A. |
| Genus | Influenzavirus A |
| Species | Influenza A virus |
| Host | Aquatic birds, human, pig, horse, seals |
| Cell Tropism | Epithelial respiratory cells |
| Associated Disease | Acute febrile respiratory tract infection |
| Mode of Transmission | Respiratory and by animal contact (in human), fecal-oral route from contaminated water (in birds ) |
| VIPR DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Orthomyxoviridae |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/negative-sense-rna-viruses-2011/w/negrna_viruses/209/orthomyxoviridae |
| Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Orthomyxoviridae |
| Paper Title | Pooled RNAi screen identifies ubiquitin ligase Itch as crucial for influenza A virus release from the endosome during virus entry |
| Author's Name | Wen-Chi Su, Yung-Chia Chen, Chung-Hsin Tseng, Paul Wei-Che Hsu, Kuo-Feng Tung, King-Song Jeng and Michael M. C. Lai |
| Journal Name | PNAS |
| Pubmed ID | 24101521 |
| Abstract | Influenza viruses, like other viruses, rely on host factors to support their life cycle as viral proteins usually "hijack," or collaborate with, cellular proteins to execute their functions. Identification and understanding of these factors can increase the knowledge of molecular mechanisms manipulated by the viruses and facilitate development of antiviral drugs. To this end, we developed a unique genome-wide pooled shRNA screen to search for cellular factors important for influenza A virus (IAV) replication. We identified an E3 ubiquitin ligase, Itch, as an essential factor for an early step in the viral life cycle. In Itch knockdown cells, the incorporation of viral ribonucleoprotein complex into endosomes was normal, but its subsequent release from endosomes and transport to the nucleus was retarded. In addition, upon virus infection, Itch was phosphorylated and recruited to the endosomes, where virus particles were located. Furthermore, Itch interacted with viral M1 protein and ubiquitinated M1 protein. Collectively, our findings unravel a critical role of Itch in mediating IAV release from the endosome and offer insights into the mechanism for IAV uncoating during virus entry. These findings also highlight the feasibility of pooled RNAi screening for exploring the cellular cofactors of lytic viruses. |
| Used Model | A549,MDCK and HEK293T cells |
| DOI | 10.1073/pnas.1312374110 |
