Fig. 3 | Nature Communications

Fig. 3

From: Monomeric ephrinB2 binding induces allosteric changes in Nipah virus G that precede its full activation

Fig. 3

Response of wildtype NiV G to binding of ephrinB2 constructs with varying length and oligomerization measured by SHG and conformational antibody binding. a EphrinB2 constructs. Listed from top to bottom are ephrinB2-Fc, ephrinB2-229, and ephrinB2-167. b Change in SHG signal of NiVG bound at 0.5 μM at 20 min following ephrinB2-Fc addition to 1.2 μM. c Binding of mAb213 to wildtype NiV G with increasing ephrinB2 construct concentration. d Binding of mAb45 to wildtype NiV G with increasing ephrinB2 construct concentration. Mean and s.d. values for SHG data are shown from a representative experiment, n = 3. Mean and s.d. values for ELISA data are shown from a representative experiment, n = 2

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