| Gene Name | MORC3 |
| HF Protein Name | MORC family CW-type zinc finger protein 3 |
| HF Function | Antiviral protein |
| Uniprot ID | Q14149 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 23515 |
| Host Factor (HF) Name in Paper | MORC3 |
| Gene synonyms | KIAA0136 NXP2 ZCWCC3 |
| Ensemble Gene ID | ENSG00000159256 |
| Ensemble Transcript | ENST00000400485 |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0003723, GO:0005654, GO:0006468, GO:0007569, GO:0008270, GO:0009791, GO:0016032, GO:0016363, GO:0016605, GO:0018105, GO:0048147, GO:0050821, GO:0051457, |
| MINT ID | N.A. |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | 610078 |
| PANTHER ID | N.A. |
| PDB ID(s) | 4QQ4, 5SVI, 5SVX, 5SVY, |
| pfam ID | PF07496, |
| 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 | MORC3, a Component of PML Nuclear Bodies, Has a Role in Restricting Herpes Simplex Virus 1 and Human Cytomegalovirus |
| Author's Name | Elizabeth Sloan, Anne Orr, Roger D. Everett |
| Journal Name | Journal Of Virology |
| Pubmed ID | 27440897 |
| Abstract | We previously reported that MORC3, a protein associated with promyelocytic leukemia nuclear bodies (PML NBs), is a target of herpes simplex virus 1 (HSV-1) ICP0-mediated degradation (E. Sloan, et al., PLoS Pathog 11:e1005059, 2015, http://dx.doi.org/10.1371/journal.ppat.1005059). Since it is well known that certain other components of the PML NB complex play an important role during an intrinsic immune response to HSV-1 and are also degraded or inactivated by ICP0, here we further investigate the role of MORC3 during HSV-1 infection. We demonstrate that MORC3 has antiviral activity during HSV-1 infection and that this antiviral role is counteracted by ICP0. In addition, MORC3s antiviral role extends to wild-type (wt) human cytomegalovirus (HCMV) infection, as its plaque-forming efficiency increased in MORC3-depleted cells. We found that MORC3 is recruited to sites associated with HSV-1 genomes after their entry into the nucleus of an infected cell, and in wt infections this is followed by its association with ICP0 foci prior to its degradation. The RING finger domain of ICP0 was required for degradation of MORC3, and we confirmed that no other HSV-1 protein is required for the loss of MORC3. We also found that MORC3 is required for fully efficient recruitment of PML, Sp100, hDaxx, and gammaH2AX to sites associated with HSV-1 genomes entering the host cell nucleus. This study further unravels the intricate ways in which HSV-1 has evolved to counteract the host immune response and reveals a novel function for MORC3 during the host intrinsic immune response. |
| Used Model | U2OS, BHK and HEK-293T cells |
| DOI | 10.1128/JVI.00621-16 |
