Egr-1 regulates expression of several viral genes and plays a crucial role in the replication of different viruses Our results from employing the EMSA and ChIP assay ( Fig. 2A) demonstrate that Egr-1 may bind ORF50P via at least two different GC-rich binding domains: at positions between 2 100 -2 76 bp (ORF50P8) and 2 2173 -2 2149 bp (ORF50P3). The results from employing the ChIP assay ( Fig. 2A) demonstrate that Egr-1 may bind ORF50P with a greater affinity at positions between 2 100 -2 76 bp (ORF50P8) compared to 2 2173 -2 2149 bp (ORF50P3). However, we did not observe any such differences in the binding affinity of Egr-1 to ORF50P3 and ORF50P8 by EMSA using IVT Egr-1 (Fig. 1B, C) . All the more, our data supports the need for Egr-1 to bind both ORF50P3 and ORF50P8 for an optimal transcriptional activity in luciferase reporter assays (Fig. 2C) . This difference observed in Egr-1 binding to both these domains could be due to one or both the reasons: (i) IVT synthesized Egr-1 was used in EMSA experiments; and (ii) the design of ChIP assay conducted in this study was not to decipher the relative binding affinity of Egr-1 to these domains; instead was performed to just confirm if Egr-1 bound these domains, in vivo.