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. 2004 May 17;199(10):1421–1431. doi: 10.1084/jem.20040191

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Copyright © 2004, The Rockefeller University Press

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Figure 1. — (A) Schematic description of EBNA1 and EBNA1ΔGA expression constructs showing localization of FLR and HPV epitopes. (B) Intracellular degradation of EBNA1-GFP in different cell types. DG75 B cells, HEK293 epithelial cells, SVMR6 keratinocytes, and HaCaT keratinocytes were transfected with expression constructs EBNA1-GFP, EBNA1ΔGA-GFP, or the control plasmid pEGFP-N1. At 36 h after transfection, the cells were degraded over a 30-h time course in the presence of 50 μg/ml cycloheximide as described in Materials and Methods. Molecular weight standards are indicated at the side of each panel. (C) Densitometric analysis of EBNA1-GFP, EBNA1ΔGA-GFP, and GFP expression. Band intensities were quantified by analysis of the imaging data and plotted as a relative percentage of the signal at time 0 for EBNA1-GFP, EBNA1ΔGA-GFP, and GFP.

Figure 1. — (A) Schematic description of EBNA1 and EBNA1ΔGA expression constructs showing localization of FLR and HPV epitopes. (B) Intracellular degradation of EBNA1-GFP in different cell types. DG75 B cells, HEK293 epithelial cells, SVMR6 keratinocytes, and HaCaT keratinocytes were transfected with expression constructs EBNA1-GFP, EBNA1ΔGA-GFP, or the control plasmid pEGFP-N1. At 36 h after transfection, the cells were degraded over a 30-h time course in the presence of 50 μg/ml cycloheximide as described in Materials and Methods. Molecular weight standards are indicated at the side of each panel. (C) Densitometric analysis of EBNA1-GFP, EBNA1ΔGA-GFP, and GFP expression. Band intensities were quantified by analysis of the imaging data and plotted as a relative percentage of the signal at time 0 for EBNA1-GFP, EBNA1ΔGA-GFP, and GFP.