| Gene Name | PIAS1 |
| HF Protein Name | E3 SUMO-protein ligase PIAS1 |
| HF Function | Antiviral protein |
| Uniprot ID | O75925 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 8554 |
| Host Factor (HF) Name in Paper | PIAS1 |
| Gene synonyms | DDXBP1 |
| Ensemble Gene ID | N.A. |
| Ensemble Transcript | ENST00000249636 [O75925-1];ENST00000545237 [O75925-2] |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0000082, GO:0000122, GO:0003677, GO:0003713, GO:0003714, GO:0005634, GO:0005654, GO:0006351, GO:0007259, GO:0007283, GO:0008022, GO:0008270, GO:0008542, GO:0016605, GO:0016607, GO:0016925, GO:0019789, GO:0019899, GO:0019904, GO:0030521, GO:0031625, GO:0032436, GO:0033235, GO:0042127, GO:0043066, GO:0045444, GO:0045893, GO:0050681, GO:0051152, GO:0060334, GO:0061665, GO:0065004, |
| MINT ID | O75925 |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | 603566 |
| PANTHER ID | N.A. |
| PDB ID(s) | 1V66, |
| pfam ID | PF14324, PF02891, |
| Drug Bank ID | N.A., |
| ChEMBL ID | N.A. |
| Organism | Homo sapiens (Human) |
| Virus Name | Human herpesvirus 1 |
| Virus Short Name | HSV1 |
| Order | Herpesvirales |
| Virus Family | Herpesviridae |
| Virus Subfamily | Alphaherpesvirinae |
| Genus | Simplexvirus |
| Species | Herpes simplex virus 1 |
| Host | Human, mammals |
| Cell Tropism | Primary site of infection: epithelial mucosal cells , latency: remains latent in sensory neurons (ganglions) |
| Associated Disease | Skin vesicles or mucosal ulcers, rarely encephalitis and meningitis |
| Mode of Transmission | Contact, saliva |
| VIPR DB link | http://www.viprbrc.org/brc/vipr_allSpecies_search.do?method=SubmitForm&decorator=herpes |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/dsdna-viruses-2011/w/dsdna_viruses/91/herpesviridae |
| Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Herpesviridae |
| Paper Title | SUMO Ligase Protein Inhibitor of Activated STAT1 (PIAS1) Is a Constituent Promyelocytic Leukemia Nuclear Body Protein That Contributes to the Intrinsic Antiviral Immune Response to Herpes Simplex Virus 1 |
| Author's Name | James R. Brown, Kristen L. Conn, Peter Wasson, Matthew Charman, Lily Tong, Kyle Grant, Steven McFarlane, Chris Boutell |
| Journal Name | Journal Of Virology |
| Pubmed ID | 27099310 |
| Abstract | Aspects of intrinsic antiviral immunity are mediated by promyelocytic leukemia nuclear body (PML-NB) constituent proteins. During herpesvirus infection, these antiviral proteins are independently recruited to nuclear domains that contain infecting viral genomes to cooperatively promote viral genome silencing. Central to the execution of this particular antiviral response is the small ubiquitin-like modifier (SUMO) signaling pathway. However, the participating SUMOylation enzymes are not fully characterized. We identify the SUMO ligase protein inhibitor of activated STAT1 (PIAS1) as a constituent PML-NB protein. We show that PIAS1 localizes at PML-NBs in a SUMO interaction motif (SIM)-dependent manner that requires SUMOylated or SUMOylation-competent PML. Following infection with herpes simplex virus 1 (HSV-1), PIAS1 is recruited to nuclear sites associated with viral genome entry in a SIM-dependent manner, consistent with the SIM-dependent recruitment mechanisms of other well-characterized PML-NB proteins. In contrast to that of Daxx and Sp100, however, the recruitment of PIAS1 is enhanced by PML. PIAS1 promotes the stable accumulation of SUMO1 at nuclear sites associated with HSV-1 genome entry, whereas the accumulation of other evaluated PML-NB proteins occurs independently of PIAS1. We show that PIAS1 cooperatively contributes to HSV-1 restriction through mechanisms that are additive to those of PML and cooperative with those of PIAS4. The antiviral mechanisms of PIAS1 are counteracted by ICP0, the HSV-1 SUMO-targeted ubiquitin ligase, which disrupts the recruitment of PIAS1 to nuclear domains that contain infecting HSV-1 genomes through mechanisms that do not directly result in PIAS1 degradation. |
| Used Model | HFt, RPE-1 and HEL cells |
| DOI | 10.1128/JVI.00426-16 |
