| Gene Name | EFNB2 |
| HF Protein Name | Ephrin-B2 |
| HF Function | Entry receptor for Nipah virus |
| Uniprot ID | P52799 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 1948 |
| Host Factor (HF) Name in Paper | EphrinB2 |
| Gene synonyms | EPLG5 HTKL LERK5 |
| Ensemble Gene ID | ENSG00000125266 |
| Ensemble Transcript | ENST00000245323 |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0001618, GO:0002042, GO:0005886, GO:0005887, GO:0005925, GO:0007155, GO:0007267, GO:0007411, GO:0008284, GO:0009653, GO:0010977, GO:0046875, GO:0048013, GO:0050920, GO:1901216, GO:2000727, |
| MINT ID | P52799 |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | 600527 |
| PANTHER ID | PTHR11304 |
| PDB ID(s) | 2HLE, 2I85, 2VSK, 2VSM, 2WO2, 3GXU, 4UF7, |
| pfam ID | PF00812, |
| Drug Bank ID | N.A., |
| ChEMBL ID | N.A. |
| Organism | Homo sapiens (Human) |
| Virus Name | Nipah virus |
| Virus Short Name | NiV |
| Order | Mononegavirales |
| Virus Family | Paramyxoviridae |
| Virus Subfamily | N.A. |
| Genus | Henipavirus |
| Species | Nipah henipavirus |
| Host | Bat and human |
| Cell Tropism | N.A. |
| Associated Disease | Fever and headache |
| Mode of Transmission | Animal bite |
| VIPR DB link | http://www.viprbrc.org/brc/vipr_allSpecies_search.do?method=SubmitForm&decorator=paramyxo |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/negative-sense-rna-viruses-2011/w/negrna_viruses/199/paramyxoviridae |
| Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Paramyxoviridae |
| Paper Title | EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus |
| Author's Name | Oscar A. Negrete, Ernest L. Levroney, Hector C. Aguilar, Andrea Bertolotti-Ciarlet, Ronen Nazarian, Sara Tajyar & Benhur Lee |
| Journal Name | Nature Letters |
| Pubmed ID | 16007075 |
| Abstract | Nipah virus (NiV) is an emergent paramyxovirus that causes fatal encephalitis in up to 70 percent of infected patients, and there is evidence of human-to-human transmission. Endothelial syncytia, comprised of multinucleated giant-endothelial cells, are frequently found in NiV infections, and are mediated by the fusion (F) and attachment (G) envelope glycoproteins. Identification of the receptor for this virus will shed light on the pathobiology of NiV infection, and spur the rational development of effective therapeutics. Here we report that ephrinB2, the membrane-bound ligand for the EphB class of receptor tyrosine kinases (RTKs), specifically binds to the attachment (G) glycoprotein of NiV. Soluble Fc-fusion proteins of ephrinB2, but not ephrinB1, effectively block NiV fusion and entry into permissive cell types. Moreover, transfection of ephrinB2 into non-permissive cells renders them permissive for NiV fusion and entry. EphrinB2 is expressed on endothelial cells and neurons, which is consistent with the known cellular tropism for NiV. Significantly, we find that NiV-envelope-mediated infection of microvascular endothelial cells and primary cortical rat neurons is inhibited by soluble ephrinB2, but not by the related ephrinB1 protein. Cumulatively, our data show that ephrinB2 is a functional receptor for NiV. |
| Used Model | 293T, Vero and HeLa cells |
| DOI | 10.1038/nature03838 |
