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. 2019 Apr 5;16:45. doi: 10.1186/s12985-019-1153-5

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© The Author(s). 2019

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 4 — The NES motif of VP1 was characterized and found to be CRM1-dependent for nuclear export to the cytoplasm. a Truncated constructions of VP1-GFP were used to identify the NES motif. Truncated fragments of VP1 (gray bars) encoding constructs fused with GFP (oval shape) were used in this study, including VP1-CD103, VP1-CD126 and VP1-IDNES3. The putative NES1 (black box), NES2 (gray box) and NES3 (white box) are shown in VP1 (gray bars). The numbers of amino acid residues are presented in the constructs. b Subcellular localization of C-terminal deleted VP1-GFP constructions (VP1-CD103 and VP1-CD126) and internal deleted VP1-IDNES3 are shown in CHO cells. All cells were fixed and stained with DAPI. b VP-GFP was treated with LMB (20 ng/mL) after 48 h of transfection. The distributions of the wild-type VP1-GFP and the truncated VP1-GFP in the cells were observed using fluorescence microscopy (400× magnification)