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. 2017 Nov 8;7:15042. doi: 10.1038/s41598-017-14886-9

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Binding of the R9-HuscFvs to native NS5A as determined by immunoprecipitation test. Lysates of HCV infected Huh7 cells treated with R9-HuscFvs were mixed with protein G resin coated with mouse anti-NS5A antibody and subjected to Western blot analysis. The preparations from lysates of HCV infected cells treated with R9-HuscFv5, R9-HuscFv9, R9-HuscFv16, R9-HuscFv19 and R9-HuscFv99 after SDS-PAGE were found to contain both NS5A (detected by mouse anti-NS5A) and R9-HuscFvs (detected by anti-E tag). The Preparation from HCV infected cells without R9-HuscFv treatment revealed only the NS5A. The results indicate that thr R9-HuscFvs bound to native NS5A.