Proteomic Identification of Dengue Virus Binding Proteins in Aedes aegypti Mosquitoes and Aedes albopictus Cells

Figure 2

Affinity chromatography of C6/36 cell extracts. Proteins were purified from C6/36 cells by affinity chromatography using DEN-2, -1, -4, or rE2-DIII-Sepharose 4B column as described in the methods section. Aliquots of 500 μL were collected from each column and proteins were acetone-precipitated. Proteins eluted from DENV-2-Sepharose 4B columns with buffer E containing 1 M NaCl are displayed in lines 1 and 2, or 0.1 M Glycine pH 2.7 in lines 3 and 4. Proteins eluted from rE2-DIII-Sepharose 4B column with 0.1 M Glycine pH 2.7 are displayed in lines 6–9. Proteins were separated by 10% SDS-PAGE and Coomassie Brilliant Blue or silver stained. The apparent molecular weights of these proteins are shown on the right side. Molecular weight markers (line 5) are shown on the left side.