Sequence basis for selectivity of ephrin-B2 ligand for Eph receptors and pathogenic henipavirus G glycoproteins.
EFNB2
EPH receptors
Hendra virus
Nipah virus
decoy receptor
deep mutational scan
henipavirus
virus entry
Journal
Journal of virology
ISSN: 1098-5514
Titre abrégé: J Virol
Pays: United States
ID NLM: 0113724
Informations de publication
Date de publication:
30 Nov 2023
30 Nov 2023
Historique:
medline:
1
12
2023
pubmed:
6
11
2023
entrez:
6
11
2023
Statut:
ppublish
Résumé
Ephrin-B2 (EFNB2) is a ligand for six Eph receptors in humans and regulates multiple cell developmental and signaling processes. It also functions as the cell entry receptor for Nipah virus and Hendra virus, zoonotic viruses that can cause respiratory and/or neurological symptoms in humans with high mortality. Here, we investigate the sequence basis of EFNB2 specificity for binding the Nipah virus attachment G glycoprotein over Eph receptors. We then use this information to engineer EFNB2 as a soluble decoy receptor that specifically binds the attachment glycoproteins of the Nipah virus and other related henipaviruses to neutralize infection. These findings further mechanistic understanding of protein selectivity and may facilitate the development of diagnostics or therapeutics against henipavirus infection.
Identifiants
pubmed: 37931130
doi: 10.1128/jvi.00621-23
pmc: PMC10688352
doi:
Substances chimiques
Ephrin-B2
0
Glycoproteins
0
Ligands
0
Viral Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0062123Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM142745
Pays : United States
Organisme : NIAID NIH HHS
ID : U19 AI142764
Pays : United States
Commentaires et corrections
Type : UpdateOf
Déclaration de conflit d'intérêts
E.P. is a shareholder and an employee of Cyrus Biotechnology, which licenses and commercializes intellectual property held by the University of Illinois for soluble decoy receptors targeting SARS-CoV-2 and HCMV. Cyrus Biotechnology had no role in the design, execution, analysis, or interpretation of the research described in this study.
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