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Fig. 2. Interaction between the cytoplasmic domains of several virus envelope glycoproteins and hDlg as determined by yeast two-hybrid assay. Yeast strain L40 was co-transformed with a plasmid encoding the fusion protein between the cytoplasmic domain of viral envelope and the LexA DNA-binding domain, and a plasmid encoding the fusion protein between hDlg (or its PDZ domains) and the Gal4 activation domain. Interaction between both fusion proteins leads to the activation of the lacZ reporter gene, which was visualized by the ß-galactosidase assay. Lamin protein was used as a negative control. (A) Interactions between the cytoplasmic domain of HTLV-1 envelope glycoproteins (CD) and the full-length hDlg protein (hDlg) or a segment of hDlg protein containing three PDZ domains (PDZ). (B) Interactions between mutated CDs and hDlg. (C) Interactions between envelope CDs of various members of the HTLV/BLV retrovirus genus and hDlg. (D) Interactions between hDlg and the CDs of Epstein-Barr virus (EBV) gp340 and rabies virus G glycoprotein.





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