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Toxins 2017, 9(8), 234; doi:10.3390/toxins9080234

Venomics of Remipede Crustaceans Reveals Novel Peptide Diversity and Illuminates the Venom’s Biological Role

1
Molecular Evolution and Systematics of Animals, Institute for Biology, University of Leipzig, Leipzig 04103, Germany
2
Department of Life Sciences, Natural History Museum, Cromwell Road, London SW7 5BD, UK
3
Centre for Advanced Imaging, University of Queensland, St. Lucia 4072, QLD, Australia
*
Authors to whom correspondence should be addressed.
Academic Editors: Nicholas R. Casewell and Syed A. Ali
Received: 27 June 2017 / Accepted: 24 July 2017 / Published: 26 July 2017
(This article belongs to the Section Animal Venoms)
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Abstract

We report the first integrated proteomic and transcriptomic investigation of a crustacean venom. Remipede crustaceans are the venomous sister group of hexapods, and the venom glands of the remipede Xibalbanus tulumensis express a considerably more complex cocktail of proteins and peptides than previously thought. We identified 32 venom protein families, including 13 novel peptide families that we name xibalbins, four of which lack similarities to any known structural class. Our proteomic data confirm the presence in the venom of 19 of the 32 families. The most highly expressed venom components are serine peptidases, chitinase and six of the xibalbins. The xibalbins represent Inhibitory Cystine Knot peptides (ICK), a double ICK peptide, peptides with a putative Cystine-stabilized α-helix/β-sheet motif, a peptide similar to hairpin-like β-sheet forming antimicrobial peptides, two peptides related to different hormone families, and four peptides with unique structural motifs. Remipede venom components represent the full range of evolutionary recruitment frequencies, from families that have been recruited into many animal venoms (serine peptidases, ICKs), to those having a very narrow taxonomic range (double ICKs), to those unique for remipedes. We discuss the most highly expressed venom components to shed light on their possible functional significance in the predatory and defensive use of remipede venom, and to provide testable ideas for any future bioactivity studies. View Full-Text
Keywords: venomics; Remipedia; crustaceans; ICK; venom; arthropods; anchialine caves venomics; Remipedia; crustaceans; ICK; venom; arthropods; anchialine caves
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

von Reumont, B.M.; Undheim, E.A.B.; Jauss, R.-T.; Jenner, R.A. Venomics of Remipede Crustaceans Reveals Novel Peptide Diversity and Illuminates the Venom’s Biological Role. Toxins 2017, 9, 234.

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