Category: Assay Development and Screening

1390-A - EphrinB2 receptor binding induces allosteric changes in Nipah virus attachment protein G

Monday, February 5, 2018
2:00 PM - 3:00 PM

Entry of Nipah virus (NiV) into host cells is triggered by the binding of its attachment protein, G, to a cellular receptor, ephrinB2 or ephrinB3. Receptor contact induces G to activate the F fusion protein, which merges the virus and host membranes. Here we show using a combination of biophysical methods (second harmonic generation, conformation-specific antibody binding, hydrogen/deuterium exchange mass spectrometry, and electron microscopy) that monomeric ephrinB2 causes allosteric changes in Nipah G without large-scale conformational changes. Different responses in NiV G are induced by monomeric ephrinB2 versus a dimeric form, suggesting that oligomerization of ephrinB2 may be a requirement for full NiV G activation. These results suggest activation of an allosteric pathway through the NiV G protein upon initial ephrinB2 contact, prior to larger scale conformational changes that lead to F-triggering. These findings may open additional modes for targeting the Nipah virus entry apparatus in vaccines and therapeutics.

Joyce JIA WEN. Wong

Postdoctoral Fellow
Stanford University
Stanford, CA

Biochemistry and Structural Biology