| Gene Name | EFNB3 |
| HF Protein Name | Ephrin-B3 |
| HF Function | Alternative entry receptor for Nipah virus |
| Uniprot ID | Q15768 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 1949 |
| Host Factor (HF) Name in Paper | EphrinB3 |
| Gene synonyms | EPLG8 LERK8 |
| Ensemble Gene ID | ENSG00000108947 |
| Ensemble Transcript | ENST00000226091 |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0001618, GO:0005005, GO:0005886, GO:0005887, GO:0007267, GO:0007399, GO:0007411, GO:0007628, GO:0016198, GO:0031295, GO:0046875, GO:0048013, GO:0050771, |
| MINT ID | N.A. |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | 602297 |
| PANTHER ID | PTHR11304 |
| PDB ID(s) | 4BKF, |
| 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 | Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virus |
| Author's Name | Oscar A. Negrete, Mike C. Wolf, Hector C. Aguilar, Sven Enterlein, Wei Wang, Elke Muhlberger, Stephen V. Su, Andrea Bertolotti-Ciarlet, Ramon Flick, Benhur Lee |
| Journal Name | PLOS Pathogens |
| Pubmed ID | 16477309 |
| Abstract | EphrinB2 was recently discovered as a functional receptor for Nipah virus (NiV), a lethal emerging paramyxovirus. Ephrins constitute a class of homologous ligands for the Eph class of receptor tyrosine kinases and exhibit overlapping expression patterns. Thus, we examined whether other ephrins might serve as alternative receptors for NiV. Here, we show that of all known ephrins (ephrinA1-A5 and ephrinB1-B3), only the soluble Fc-fusion proteins of ephrinB3, in addition to ephrinB2, bound to soluble NiV attachment protein G (NiV-G). Soluble NiV-G bound to cell surface ephrinB3 and B2 with subnanomolar affinities (Kd = 0.58 nM and 0.06 nM for ephrinB3 and B2, respectively). Surface plasmon resonance analysis indicated that the relatively lower affinity of NiV-G for ephrinB3 was largely due to a faster off-rate (K(off) = 1.94 x 10(-3) s(-1) versus 1.06 x 10(-4) s(-1) for ephrinB3 and B2, respectively). EphrinB3 was sufficient to allow for viral entry of both pseudotype and live NiV. Soluble ephrinB2 and B3 were able to compete for NiV-envelope-mediated viral entry on both ephrinB2- and B3-expressing cells, suggesting that NiV-G interacts with both ephrinB2 and B3 via an overlapping site. Mutational analysis indicated that the Leu-Trp residues in the solvent exposed G-H loop of ephrinB2 and B3 were critical determinants of NiV binding and entry. Indeed, replacement of the Tyr-Met residues in the homologous positions in ephrinB1 with Leu-Trp conferred NiV receptor activity to ephrinB1. Thus, ephrinB3 is a bona fide alternate receptor for NiV entry, and two residues in the G-H loop of the ephrin B-class ligands are critical determinants of NiV receptor activity. |
| Used Model | CHO-pgsA745 |
| DOI | 10.1371/journal.ppat.0020007 |
