Virus Name | Vesicular stomatitis Indiana virus |
Virus Short Name | VSV |
Order | Mononegavirales |
Virus Family | Rhabdoviridae |
Virus Subfamily | N.A. |
Genus | Vesiculovirus |
Species | Indiana vesiculovirus |
Host | Human, cattle, horse, swine, sandflies, blackflies |
Cell Tropism | N.A. |
Associated Disease | Vesicular diseases, encephalitis |
Mode of Transmission | Mostely by sandflies |
VIPR DB link | https://www.viprbrc.org/brc/vipr_allSpecies_search.spg?method=SubmitForm&decorator=rhabdo |
ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/negative-sense-rna-viruses-2011/w/negrna_viruses/201/rhabdoviridae |
Virus Host DB link | N.A. |
Paper Title | Double-stranded RNA deaminase ADAR1 increases host susceptibility to virus infection |
Author's Name | Yongzhan Nie, Graeme L. Hammond, and Jing-Hua Yang |
Journal Name | Journal Of Virology |
Pubmed ID | 17079286 |
Abstract | The RNA-editing enzyme ADAR1 is a double-stranded RNA (dsRNA) binding protein that modifies cellular and viral RNA sequences by adenosine deamination. ADAR1 has been demonstrated to play important roles in embryonic erythropoiesis, viral response, and RNA interference. In human hepatitis virus infection, ADAR1 has been shown to target viral RNA and to suppress viral replication through dsRNA editing. It is not clear whether this antiviral effect of ADAR1 is a common mechanism in response to viral infection. Here, we report a proviral effect of ADAR1 that enhances replication of vesicular stomatitis virus (VSV) through a mechanism independent of dsRNA editing. We demonstrate that ADAR1 interacts with dsRNA-activated protein kinase PKR, inhibits its kinase activity, and suppresses the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha) phosphorylation. Consistent with the inhibitory effect on PKR activation, ADAR1 increases VSV infection in PKR+/+ mouse embryonic fibroblasts however, no significant effect was found in PKR-/- cells. This proviral effect of ADAR1 requires the N-terminal domains but does not require the deaminase domain. These findings reveal a novel mechanism of ADAR1 that increases host susceptibility to viral infection by inhibiting PKR activation. |
Used Model | HEK 293T, NIH 3T3, SGC7901 and N18 cells |
DOI | 10.1128/JVI.01527-06 |