| Gene Name | PHF13 |
| HF Protein Name | PHD finger protein 13 |
| HF Function | Virus restriction factor |
| Uniprot ID | Q86YI8 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 148479 |
| Host Factor (HF) Name in Paper | SPOC1 |
| Gene synonyms | N.A. |
| Ensemble Gene ID | ENSG00000116273 |
| Ensemble Transcript | ENST00000377648 |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0000278, GO:0003682, GO:0005634, GO:0005654, GO:0006325, GO:0007059, GO:0007076, GO:0035064, GO:0046872, GO:0051301, |
| MINT ID | N.A. |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | N.A. |
| PANTHER ID | N.A. |
| PDB ID(s) | 3O70, 3O7A, |
| pfam ID | PF00628, |
| Drug Bank ID | N.A., |
| ChEMBL ID | CHEMBL1764945 |
| Organism | Homo sapiens (Human) |
| Virus Name | Human adenovirus 3 |
| Virus Short Name | HAdV-5 |
| Order | Unassigned |
| Virus Family | Adenoviridae |
| Virus Subfamily | N.A. |
| Genus | Mastadenovirus |
| Species | Human mastadenovirus C |
| Host | Human, mammals |
| Cell Tropism | Epithelial cells |
| Associated Disease | Very common human infection, estimated to be responsible for between 2% and 5% of all respiratory infections. usually mild respiratory, gastrointestinal and eye infections. |
| Mode of Transmission | Respiratory, fecal-oral |
| VIPR DB link | N.A. |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/dsdna-viruses-2011/w/dsdna_viruses/93/adenoviridae |
| Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Adenoviridae |
| Paper Title | Human Adenovirus Core Protein V Is Targeted by the Host SUMOylation Machinery To LimitEssential Viral Functions |
| Author's Name | Nora Freudenberger,Tina Meyer, Peter Groitl, Thomas Dobner, Sabrina Schreiner |
| Journal Name | Journal Of Virology |
| Pubmed ID | 29167340 |
| Abstract | Human adenoviruses (HAdV) are nonenveloped viruses containing a linear, double-stranded DNA genome surrounded by an icosahedral capsid. To allow proper viral replication, the genome is imported through the nuclear pore complex associated with viral core proteins. Until now, the role of these incoming virion proteins during the early phase of infection was poorly understood. The core protein V is speculated to bridge the core and the surrounding capsid. It binds the genome in a sequence-independent manner and localizes in the nucleus of infected cells, accumulating at nucleoli. Here, we show that protein V contains conserved SUMO conjugation motifs (SCMs). Mutation of these consensus motifs resulted in reduced SUMOylation of the protein thus, protein V represents a novel target of the host SUMOylation machinery. To understand the role of protein V SUMO posttranslational modification during productive HAdV infection, we generated a replication-competent HAdV with SCM mutations within the protein V coding sequence. Phenotypic analyses revealed that these SCM mutations are beneficial for adenoviral replication. Blocking protein V SUMOylation at specific sites shifts the onset of viral DNA replication to earlier time points during infection and promotes viral gene expression. Simultaneously, the altered kinetics within the viral life cycle are accompanied by more efficient proteasomal degradation of host determinants and increased virus progeny production than that observed during wild-type infection. Taken together, our studies show that protein V SUMOylation reduces virus growth hence, protein V SUMOylation represents an important novel aspect of the host antiviral strategy to limit virus replication and thereby points to potential intervention strategies.IMPORTANCEÂ Many decades of research have revealed that HAdV structural proteins promote viral entry and mainly physical stability of the viral genome in the capsid. Our work over the last years showed that this concept needs expansion as the functions are more diverse. We showed that capsid protein VI regulates the antiviral response by modulation of the transcription factor Daxx during infection. Moreover, core protein VII interacts with SPOC1 restriction factor, which is beneficial for efficient viral gene expression. Here, we were able to show that core protein V also represents a novel substrate of the host SUMOylation machinery and contains several conserved SCMs mutation of these consensus motifs reduced SUMOylation of the protein. Unexpectedly, we observed that introducing these mutations into HAdV promotes adenoviral replication. In conclusion, we offer novel insights into adenovirus core proteins and provide evidence that SUMOylation of HAdV factors regulates replication efficiency. |
| Used Model | H1299 and Hela cells |
| DOI | 10.1128/JVI.01451-17 |
