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dc.contributor.authorRichter, Sandy
dc.contributor.authorHelm, Conrad
dc.contributor.authorMeunier, Frederic A
dc.contributor.authorHering, Lars
dc.contributor.authorCampbell, Lahcen I
dc.contributor.authorDrukewitz, Stephan H
dc.contributor.authorUndheim, Eivind AB
dc.contributor.authorJenner, Ronald
dc.contributor.authorSchiavo, Giampietro
dc.contributor.authorBleidorn, Christoph
dc.date.accessioned2022-06-17T13:47:11Z
dc.date.available2022-06-17T13:47:11Z
dc.date.issued2017-03-04
dc.date.submitted2016-10-23
dc.identifier.citationRichter, S., Helm, C., Meunier, F.A. et al. Comparative analyses of glycerotoxin expression unveil a novel structural organization of the bloodworm venom system. BMC Evol Biol 17, 64 (2017). https://doi.org/10.1186/s12862-017-0904-4en_US
dc.identifier.issn1471-2148
dc.identifier.doi10.1186/s12862-017-0904-4
dc.identifier.urihttp://hdl.handle.net/10141/622982
dc.description.abstractBackground: We present the first molecular characterization of glycerotoxin (GLTx), a potent neurotoxin found in the venom of the bloodworm Glycera tridactyla (Glyceridae, Annelida). Within the animal kingdom, GLTx shows a unique mode of action as it can specifically up-regulate the activity of Ca<sub>v</sub>2.2 channels (N-type) in a reversible manner. The lack of sequence information has so far hampered a detailed understanding of its mode of action. Results: Our analyses reveal three ~3.8 kb GLTx full-length transcripts, show that GLTx represents a multigene family, and suggest it functions as a dimer. An integrative approach using transcriptomics, quantitative real-time PCR, in situ hybridization, and immunocytochemistry shows that GLTx is highly expressed exclusively in four pharyngeal lobes, a previously unrecognized part of the venom apparatus. Conclusions: Our results overturn a century old textbook view on the glycerid venom system, suggesting that it is anatomically and functionally much more complex than previously thought. The herein presented GLTx sequence information constitutes an important step towards the establishment of GLTx as a versatile tool to understand the mechanism of synaptic function, as well as the mode of action of this novel neurotoxin.en_US
dc.language.isoenen_US
dc.publisherSpringer Science and Business Media LLCen_US
dc.rightsopenAccessen_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleComparative analyses of glycerotoxin expression unveil a novel structural organization of the bloodworm venom systemen_US
dc.typeJournal Articleen_US
dc.identifier.eissn1471-2148
dc.identifier.journalBMC Evolutionary Biologyen_US
dc.date.updated2022-06-15T12:57:36Z
dc.identifier.volume17en_US
dc.identifier.issue1en_US
dc.identifier.startpage64-en_US
elements.import.authorRichter, Sandy
elements.import.authorHelm, Conrad
elements.import.authorMeunier, Frederic A
elements.import.authorHering, Lars
elements.import.authorCampbell, Lahcen I
elements.import.authorDrukewitz, Stephan H
elements.import.authorUndheim, Eivind AB
elements.import.authorJenner, Ronald A
elements.import.authorSchiavo, Giampietro
elements.import.authorBleidorn, Christoph
dc.description.nhmCopyright © The Author(s). 2017 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.en_US
dc.description.nhmNHM Repository
dc.subject.nhmannelidaen_US
dc.subject.nhmglyceridaeen_US
dc.subject.nhmcalcium channelen_US
dc.subject.nhmneurotoxinen_US
dc.subject.nhmGLTxen_US
dc.subject.nhmvenom systemen_US


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