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. 2019 Jun 5;16(7):3145–3156. doi: 10.1021/acs.molpharmaceut.9b00360

Figure 2.

Figure 2

VUN100 binds to the N-terminus and ECL3 loop of US28. (A) Immunofluorescence microscopy of the binding of VUN100 to Mock, US28 wild-type (US28 WT), N-terminus truncated US28 (US28-Δ2-22), and US28 with mutation of the tyrosine at position 16 to a phenylalanine (US28 Y16F). US28 was detected using an anti-US28 antibody (US28). VUN100 binding was detected using the Myc-tag and an anti-Myc antibody (VUN100). (B) Detection of surface and total expression of HA-tagged US28 wildtype (US28 WT) and HA-tagged US28 chimeras with the CL1–3 loop being substituted by the corresponding loops of CCR5. Receptor expression was detected by the N-terminal HA-tag. (C) Immunofluorescence microscopy of the binding of VUN100 to Mock transfected or US28 chimeras with the ECL1–3 loop being substituted by the corresponding loops of CCR5. US28 was detected using an anti-US28 antibody (US28). VUN100 binding was detected using the Myc-tag and an anti-Myc antibody (VUN100). (D) Binding ELISA of different concentrations of VUN100 to membranes of HEK293T cells transfected with wild-type US28 (WT), US28 Y16F (Y16F), US28 ECL1-CCR5 chimera (ECL1), US28 ECL3-CCR5 chimera (ECL3), and US28-Δ2-22 (Δ2-22).