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. 2017 Sep 12;7:11282. doi: 10.1038/s41598-017-11717-9

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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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Protein profile and antigenicity of the Cyt1Aa-BinA chimera. Inclusion bodies were purified from Bacillus thuringiensis subsp. israelensis 4Q7 strains producing (A) Cyt1Aa (4Q7/pWF45; lanes 1, 2), Cyt1A-BinA (4Q7/pBU-cyt1Aa-binA; lanes 3, 4), (B) Cyt1Aa and BinAB (4Q7/45S1; lanes 1, 2) or Cyt1A-BinA (4Q7/pBU-cyt1A-binA; lanes 3, 4). Inclusions were solubilized and fractionated by SDS-PAGE in a 10% gel and electroblotted for Western analysis using rabbit anti-Cyt1Aa and anti-BinA antibodies (Ab). Lanes 1, 2, and 3, 4, respectively, 0.75 μg and 1.5 μg of protein; molecular masses: Cyt1Aa, 27.2 kDa; BinA, 42 kDa; BinB, 52 kDa; and Cyt1Aa-BinA 69.6 kDa. (C) SDS-PAGE demonstrating proteolytic cleavage of Cyt1Aa-BinA by trypsin, with Cyt1Aa as a control. Purified parasporal inclusions were solubilized in 50 mM NaOH, supernatants collected and neutralized with HCl, and digested with the enzyme at 28 °C. Untreated samples, 1.5 hr (lane 1), and trypsin-treated samples, 0.5 hr (lane 2) and 1.5 hr (lane 3). (D) Midgut histopathology caused by Cyt1Aa-BinA chimera in fourth instars of Culex quinquefasciatus 8 hours post-treatment at the LC₉₅ concentration; Control midgut epithelium, (i) and (ii), respectively, 100x and 400x magnification. Midgut epithelium of a treated larva (iii) and (iv), respectively 100x and 600x magnification. Note the vacuoles in cells designated by arrows in D (iv) that have sloughed from the midgut basement membrane (C, 100x; D, 600x). The central circular area in A is the food column surrounded by the peritrophic membrane. MW, protein molecular mass standards; kDa, kilodaltons.