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. 2016 Dec 2;6:38372. doi: 10.1038/srep38372

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Copyright © 2016, The Author(s)

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(A) Purified vimentin proteins of the rod (a.a. 102–410) (Lane 1), tail (a.a. 411–466) (Lane 3), and head (a.a. 1–101) (Lane 4) domains, and the full-length vimentin (Lane 5) were analyzed by SDS-PAGE. Protein sizes were indicated on the left. (B) Vimentin–binding ELISA. The binding levels of vimentin head, rod, and tail domain proteins, and the full-length protein with DENV-2 or DENV-2 EDIII protein, respectively, showed that both DENV-2 EDIII protein and DENV-2 could specifically bind to vimentin rod and the full-length vimentin proteins. BSA served as negative control and PBS served as blank control. (C) Protein-binding levels were represented by reads of the ELISA plates at 405 nm on a VERSAmax tunable microplate reader. All experiments were repeated in triplicate and reported as average and S.D.; P-values were indicated versus BSA negative control. * indicates P < 0.01.