Fig. 4: Interaction and functional effects of the HSV1 gD 24AA homologous loop peptide with L-AChBP and the α7 nAChR.
From: HSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptors
a Binding to the L –AChBP, SPR binding data at five different concentrations (31 μM, 62 μM, 125 μM, and 250 μM) of the 24AA HSV1 gD peptide. L-AChBP is the ligand, and the 24AA HSV1 gD peptide is the analyte. The analyte was injected for 4 min at a flow rate of 25 μL/min. Binding data was fit to a 1:1 binding model (Kd = 4.32 × 10-4 ± 3.99 × 10-4 M.). b Functional effects of the 24 AA gD peptide on α7 nAChRs expressed in Xenopus oocytes. The 24AA fragment of HSV1 gD inhibited acetylcholine-induced responses of α7 nAChRs in a dose-dependent manner. Four different concentrations of the putative binding loop peptide (10 μM, 30 μM, 100 μM, and 300 μM) produced AUCs of 666, 634, 647, and 140 μA·ms respectively. c Dose response curve for inhibition of nicotinic-induced responses by the 24AA loop peptide of HSV1gD. Oocytes were co-exposed to 100 µM ACh and the 24AA peptide. AUC was determined for each trace, and results of at least 4 oocytes were pooled to obtain the data shown in the figure (IC50 = 157 µM, 95% CI:132 µM to 186 µM).
