Recombinant Nipah virus Glycoprotein G (G)

1. G and the fusion protein F are both crucial glycoproteins located on the surface of the virus envelope. [review] PMID:29963835
2. the binding of the viral attachment protein G to its host receptor ephrinB2 was studied and showed monomeric and dimeric receptors activate distinct conformational changes in G. PMID:28974687
3. Data suggest that fusion of Nipah viruses with host cells is facilitated by two of viral membrane proteins, the G protein and the F protein; G head domain binds to human ephrins B2 and B3 altering conformational density of entire G head domain. PMID:24615845
4. Authors identified a G stalk C-terminal region (amino acids 159 to 163) that is important for multiple G functions, including G tetramerization, conformational integrity, G-F interactions, receptor-induced conformational changes in G, and F triggering. PMID:25428863
5. Cysteine cluster in the G protein is involved in stabilizing a unique microdomain critical for triggering fusion. PMID:22496210
6. Results indicated that the G-H loop of ephrin-B2 was indeed critical for the interaction between ephrin-B2 and Nipah virus-G. PMID:21632558
7. the G protein appeared to be constitutively internalized with the bulk flow during membrane turnover PMID:15731282
8. sNiV-G binds to ephrinB3 with a 30-fold higher affinity than that of sHeV-G. PMID:17652392
9. report the crystal structures of the NiV-G both in its receptor-unbound state and in complex with ephrin-B3, providing, to our knowledge, the first view of a paramyxovirus attachment complex in which a cellular protein is used as the virus receptor PMID:18632560

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KEGG: vg:920955