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. 2022 Mar 23;13:794779. doi: 10.3389/fimmu.2022.794779

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Copyright © 2022 Wang, Xie, Huang, Li, Liu, Chen and Wang

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Sequence comparison of Tatritin, Tachystatins, and Neurotoxins from spider venoms. (A) Amino acid sequence alignment of Tatritin and Tachystatins. Conserved cysteines are indicated in large boldface letters. Lines show the identical pattern of disulfide bonds in Tatritin and Tachystatins. (B) Alignment of the amino acid sequence of Tatritin with those of insecticidal peptides from venom of the spiders. Conserved cysteines are indicated in large boldface letters. Lines show the identical pattern of disulfide bonds in Tatritin and Neurotoxins. (C) β-Sheet structural models of the C-terminal regions of Tatritin and Tachystatin C. Solid/dashed lines indicate side chains pointing out of/into the plane of the diagram. Basic and hydrophobic amino acid residues are indicated in underline and red highlight, respectively. The numbers indicate the positions of amino acid residues in the mature peptide.