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Figure 1 | Virology Journal

Figure 1

From: Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein

Figure 1

CTMP-7 is a VP26 interacting protein. a. Binding assay of the proteins and VP26. The positive control was the fusion yeast containing pGBK-p53 and pACT-LT. The negative control was the fusion yeast containing pGBK-Lam and pACT-LT. b. Amino acid sequence features of CTMP-7. The amino acid sequence of CTMP-7 contains the typical tetraspanin-enriched domain with four transmembrane regions (shown in red) and a topological domain (shown in black). c. Co-immunoprecipitation of the VP26 and CTMP-7 interaction complex and immunoblot by anti-CTMP-7 antibody. Vero cells transfected by VP26 and CTMP gene and labeled with 35S-methionine were lysed in RIPA buffer and interacted with anti-VP26 or anti-CTMP antibodies. Lane 1: The immunoprecipitated complexes of cells co-transfected with VP26 and CTMP genes by anti-VP26 antibody; Lane 2: The immunoprecipitated complexes of cells co-transfected with VP26 and CTMP genes by anti-CTMP-7 antibody. Lane 3: The immunoprecipitated complexes of cells transfected with pcDNA mock by anti-VP26 antibody; and Lane 4: The immunoprecipitated complexes of cells transfected with pcDNA mock by anti-CTMP-7 antibody. Lane 5: Control cells lysate; Lane 6: Negative control with normal mouse IgG. d. Mapping the region of CTMP-7 interaction with VP26. The plasmids encoding CTMP-7 amino acid residues 1-61, 61-150 and 150-249 were constructed and transfected into yeast Y187. These transfected Y187 clones were fused with AH109 transfected with pGBK-VP26. These fused clones were identified on QDO plates and their β-galactosidase activity was analyzed.

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