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. 2018 Oct 15;8:15276. doi: 10.1038/s41598-018-33215-2

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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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Comparison of Tv1 and Tsu1.1 teretoxins. (A) The bioinformatic pipeline used to identify Tsu1.1. The orange box indicates the initial steps to generate reads through next-generation sequencing (NGS), the green shows the process to assemble the terebrid venom gland transcriptome, and the purple represents the final steps that lead to the discovery of teretoxins. (B) Shell images of Terebra variegata (left) and Terebra subulata (right), scale bar represents ~1 cm, followed by the sequence of each venom peptide, with cysteines highlighted in red, followed by the NMR structure of Tv1⁴⁶ and the predicted I-TASSER structure of Tsu1.1. (C) An alignment of Tv1 and conotoxins in the M-superfamily, followed by an alignment of Tsu1.1 and conotoxins in the A-superfamily. Green represents shared amino acids, while red represents shared cysteine framework.