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dc.contributor.authorvon Reumont, Björn
dc.contributor.authorUndheim, Eivind
dc.contributor.authorJauss, Robin-Tobias
dc.contributor.authorJenner, Ronald
dc.date.accessioned2022-06-17T14:53:55Z
dc.date.available2022-06-17T14:53:55Z
dc.date.issued2017-07-26
dc.date.submitted2017-06-27
dc.identifier.citationVon 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. https://doi.org/10.3390/toxins9080234en_US
dc.identifier.issn2072-6651
dc.identifier.doi10.3390/toxins9080234
dc.identifier.urihttp://hdl.handle.net/10141/622986
dc.description.abstractWe 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.en_US
dc.language.isoenen_US
dc.publisherMDPI AGen_US
dc.rightsopenAccessen_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleVenomics of Remipede Crustaceans Reveals Novel Peptide Diversity and Illuminates the Venom’s Biological Roleen_US
dc.typeJournal Articleen_US
dc.identifier.eissn2072-6651
dc.identifier.journalToxinsen_US
dc.date.updated2022-06-15T12:49:06Z
dc.identifier.volume9en_US
dc.identifier.issue8en_US
dc.identifier.startpage234-234en_US
elements.import.authorvon Reumont, Björn
elements.import.authorUndheim, Eivind
elements.import.authorJauss, Robin-Tobias
elements.import.authorJenner, Ronald
dc.description.nhmThis 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. The attached file is the published version of the article.en_US
dc.description.nhmNHM Repository
dc.subject.nhmvenomicsen_US
dc.subject.nhmremipediaen_US
dc.subject.nhmcrustaceansen_US
dc.subject.nhmICKen_US
dc.subject.nhmvenomen_US
dc.subject.nhmathropodsen_US
dc.subject.nhmanchialine cavesen_US


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