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. 2019 Feb 7;9:1634. doi: 10.1038/s41598-018-37647-8

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© The Author(s) 2019

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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Bioinformatic detection of BoNT-related genes in microbial genomes. (a) PCoA ordination of pairwise percent similarities reveals relationships between the sequence families surveyed in this study. A large family of ADP-ribosyltransferase toxins, including diphtheria toxin-like proteins and a large family of predicted toxins from entomopathogenic fungi possess similarity only over the translocase domain (cluster I). M91 peptidases group separately (cluster II). BoNT and NTNH form distinct groups, with more divergent relatives such as the Weissella BoNT-like protein clustering outside them. The next closest relatives are the BoNT-like toxins found in Chryseobacterium, followed by putative toxins from other Actinobacteria (cluster III), which span the distance between groups, having similarities to each. Notably, genes encoding M. chelonae BoNT-like proteins appear to be split into two components (one encoding the “light chain” M27-like peptidase, and the second encoding the “heavy chain” translocation domain and receptor-binding domain). (b) InterPro domain predictions for Chryseobacterium piperi BoNT-like protein Cp1 (WP_034687872.1), revealing a similar architecture to BoNT. The translocase domain is annotated as diphtheria-like, and contains two predicted transmembrane helices. (c) Comparison of BoNT/A1 peptidase domain to C. piperi putative peptidases and peptidases in the MEROPS database. Except for peptidase M27 (not pictured), the peptidases from Chryseobacterium produce the highest-scoring global alignments, followed by peptidase M91. Both C. piperi peptidases and M91 peptidases score higher than all other known peptidase families.