Comparative analyses of glycerotoxin expression unveil a novel structural organization of the bloodworm venom system

التفاصيل البيبلوغرافية
العنوان: Comparative analyses of glycerotoxin expression unveil a novel structural organization of the bloodworm venom system
المؤلفون: Richter, S, Helm, C, Meunier, FA, Hering, L, Campbell, LI, Drukewitz, SH, Undheim, EAB, Jenner, RA, Schiavo, G, Bleidorn, C
المساهمون: German Research Foundation, European Commission, University College London, Cancer Research UK, Leipzig University
المصدر: Digital.CSIC. Repositorio Institucional del CSIC
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BMC Evolutionary Biology
بيانات النشر: BioMed Central, 2017.
سنة النشر: 2017
مصطلحات موضوعية: GLTx, Venom system, Venoms, Annelida, Glyceridae, Neurotoxins, Helminth Proteins, Calcium channels, Calcium channel, Multigene Family, Animals, Amino Acid Sequence, Neurotoxin, Ecology, Evolution, Behavior and Systematics, Research Article
الوصف: © The Author(s).
[Background]: 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 Cav2.2 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.
This work was supported by Cancer Research UK [GS], a Wellcome Trust Senior Investigator Award (107116/Z/15/Z) [GS], and University College London [GS]. This work was further supported by the German Research Foundation (DFG; grant BL787/7-1) and an EU ASSEMBLE grant (No. 227799; http://www.assemblemarine.org) to CB. We acknowledge support from the German Research Foundation (DFG) and Universität Leipzig within the program of Open Access Publishing.
URL الوصول: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::37d8b9aa32ba14487d27d87182176bac
http://hdl.handle.net/10261/195016
حقوق: OPEN
رقم الأكسشن: edsair.pmid.dedup....37d8b9aa32ba14487d27d87182176bac
قاعدة البيانات: OpenAIRE