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. 2018 Apr 16;8:6030. doi: 10.1038/s41598-018-24463-3

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© The Author(s) 2018

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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3B12A scFv-CMA is degraded by both proteasome and autophagy proteolytic pathways. (a) Illustrative domain profiles of 3B12A scFv for VH_VL-Myc with or without proteolytic signals including CL1 for proteasomes and chaperone-mediated autophagy (CMA) for autophagosomes. (b) Protein degradation chase assay of C4F6 scFv (C4F6-VH_VL), 3B12A scFv (VH_VL), 3B12A scFv-CL1 (VH_VL-CL1) and 3B12A scFv-CMA (VH_VL-CMA) in HEK293A cells. (c) Quantitative analysis of (b) Each data point was obtained by normalisation to actin. Differences were evaluated by one-way ANOVA (mean ± SD from three independent experiments; *p < 0.05, ***p < 0.005 and ****p < 0.001). N.S. indicates not significant. ‘remaining scFv (%)’ indicates ‘the % signal compared with time 0’. (d) Protein degradation chase assay of 3B12A-VH and 3B12A-VL in HEK293A cells. (e) Quantified analysis of (d) Each data point was obtained by normalisation to actin. Differences were evaluated by one-way ANOVA (mean ± SD from three independent experiments; **p < 0.01 and ***p < 0.005).