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

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 2.2 channels...

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Bibliographic Details
Published in:	BMC evolutionary biology 2017-03, Vol.17 (1), p.64, Article 64
Main Authors:	Richter, Sandy, Helm, Conrad, Meunier, Frederic A, Hering, Lars, Campbell, Lahcen I, Drukewitz, Stephan H, Undheim, Eivind A B, Jenner, Ronald A, Schiavo, Giampietro, Bleidorn, Christoph
Format:	Article
Language:	eng
Subjects:	Amino Acid Sequence Animals Annelida - genetics Annelida - physiology Helminth Proteins - biosynthesis Helminth Proteins - chemistry Helminth Proteins - genetics Multigene Family Neurotoxins - biosynthesis Neurotoxins - chemistry Venoms - biosynthesis Venoms - chemistry Venoms - genetics
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Summary:	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 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. 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. 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.
ISSN:	1471-2148 1471-2148