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. 2021 Jul 16;12:4357. doi: 10.1038/s41467-021-24574-y

Fig. 2. VUN103 inhibits US28 signaling by binding to the ICL2 loop.

Fig. 2

a US28-mediated inositol phosphate (IP) accumulation of HEK293T cells expressing US28 and increasing amounts of VUN103, VUN103-mVenus (VUN103 mV), non-US28 targeting intrabody (Irr Nb) or non-US28 targeting intrabody-mVenus (Irr Nb mV) (n = 3 independent experiments). b–d Effect of US28 (No Nb) and US28 co-transfected with Irr Nb mV and VUN103 mV on NFAT activation (b), NF-κB activation (c) and STAT3 activation (d). Levels were normalized to cells transfected only with the reporter gene construct (n = 3 independent experiments). e US28-mediated IP accumulation of HEK293T cells expressing US28 (No Nb), US28 and Irr Nb mV, VUN103 mV, or Nb7-mVenus (Nb7 mV) (n = 3 independent experiments). f, g US28-mediated IP accumulation of HEK293T cells expressing HA-US28 wildtype (US28 WT), HA-US28 lacking a C-tail (US28 Δ300, f or an HA-US28 chimera with the ICL2 loop substituted with the corresponding ICL2 loop of CCR5 (US28 ICL2 CCR5, (g)). Cells expressed the US28 construct (No Nb) alone or in co-expressed with Irr Nb mV or VUN103 mV. All inositol phosphate accumulation levels were normalized to cells expressing US28 WT and no Nb-mVenus construct (n = 3 independent experiments). All data are plotted as mean ± SD. Statistical analyses were performed using unpaired two-tailed t-test. ns, p > 0.05. Source data are provided as a Source Data file.