| Gene Name | FCN1 |
| HF Protein Name | Ficolin-1 |
| HF Function | Enhances Ebola Virus infection |
| Uniprot ID | O00602 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 2219 |
| Host Factor (HF) Name in Paper | FCN1 |
| Gene synonyms | FCNM |
| Ensemble Gene ID | ENSG00000085265 |
| Ensemble Transcript | ENST00000371806 |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0001664, GO:0001867, GO:0002752, GO:0004252, GO:0005576, GO:0005581, GO:0006956, GO:0007186, GO:0008329, GO:0030246, GO:0031232, GO:0033691, GO:0034394, GO:0034774, GO:0043312, GO:0043654, GO:0046597, GO:0046872, GO:1904813, GO:2000484, |
| MINT ID | O00602 |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | 601252 |
| PANTHER ID | N.A. |
| PDB ID(s) | 2D39, 2JHH, 2JHI, 2JHK, 2JHL, 2JHM, 2WNP, |
| pfam ID | PF01391, PF00147, |
| Drug Bank ID | N.A., |
| ChEMBL ID | N.A. |
| Organism | Homo sapiens (Human) |
| Virus Name | Zaire ebolavirus |
| Virus Short Name | ZEBOV |
| Order | Bunyavirales |
| Virus Family | Filoviridae |
| Virus Subfamily | N.A. |
| Genus | Ebolavirus |
| Species | Zaire ebolavirus |
| Host | Bats, human and primates |
| Cell Tropism | N.A. |
| Associated Disease | Hemorragic fever |
| Mode of Transmission | Zoonosis, contact with body fluids |
| VIPR DB link | http://www.viprbrc.org/brc/vipr_allSpecies_search.do?method=SubmitForm&decorator=filo |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/negative-sense-rna-viruses-2011/w/negrna_viruses/197/filoviridae |
| Virus Host DB link | N.A. |
| Paper Title | Enhancement of Ebola virus infection via ficolin-1 interaction with the mucin domain of GP glycoprotein |
| Author's Name | Anne-Laure Favier, Evelyne Gout, Olivier Reynard, Olivier Ferraris, Jean-Philippe Kleman, Viktor Volchkov, Christophe Peyrefitte, Nicole M. Thielens |
| Journal Name | Journal Of Virology |
| Pubmed ID | 26984723 |
| Abstract | Ebola virus infection requires the surface viral glycoprotein to initiate entry into the target cells. The trimeric glycoprotein is a highly glycosylated viral protein which has been shown to interact with host C-type lectin receptors and the soluble complement recognition protein mannose-binding lectin, thereby enhancing viral infection. Similarly to mannose-binding lectin, ficolins are soluble effectors of the innate immune system that recognize particular glycans at the pathogen surface. In this study, we demonstrate that ficolin-1 interacts with the Zaire Ebola virus (EBOV) glycoprotein, and we characterized this interaction by surface plasmon resonance spectroscopy. Ficolin-1 was shown to bind to the viral glycoprotein with a high affinity. This interaction was mediated by the fibrinogen-like recognition domain of ficolin-1 and the mucin-like domain of the viral glycoprotein. Using a ficolin-1 control mutant devoid of sialic acid-binding capacity, we identified sialylated moieties of the mucin domain to be potential ligands on the glycoprotein. In cell culture, using both pseudotyped viruses and EBOV, ficolin-1 was shown to enhance EBOV infection independently of the serum complement. We also observed that ficolin-1 enhanced EBOV infection on human monocyte-derived macrophages, described to be major viral target cells,. Competition experiments suggested that although ficolin-1 and mannose-binding lectin recognized different carbohydrate moieties on the EBOV glycoprotein, the observed enhancement of the infection likely depended on a common cellular receptor/partner. In conclusion, ficolin-1 could provide an alternative receptor-mediated mechanism for enhancing EBOV infection, thereby contributing to viral subversion of the host innate immune system. |
| Used Model | Vero E6 cell and 293T cells |
| DOI | 10.1128/JVI.00232-16 |
