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Comparative analyses of glycerotoxin expression unveil a novel structural organization of the bloodworm venom system
Richter, S.; Helm, C.; Meunier, F.A.; Hering, L.; Campbell, L.I.; Drukewitz, S.H.; Undheim, E.A.B.; Jenner, R.A.; Schiavo, G.; Bleidorn, C. (2017). Comparative analyses of glycerotoxin expression unveil a novel structural organization of the bloodworm venom system. BMC Evol. Biol. 17. https://dx.doi.org/10.1186/s12862-017-0904-4
In: BMC Evolutionary Biology. BioMed Central: London. ISSN 1471-2148; e-ISSN 1471-2148, meer
Peer reviewed article  
Beschikbaar in  Auteurs 
Trefwoorden
    Data
    Marine Sciences
    Marine Sciences > Marine Genomics
    Scientific Community
    Scientific Publication
    Marien/Kust
Author keywords
    Annelida; Glyceridae; Calcium channel; Neurotoxin; GLTx; Venom system
Project Top | Auteurs 
  • Association of European marine biological laboratories, meer
Auteurs  Top 
  • Richter, S.
  • Helm, C.
  • Meunier, F.A.
  • Hering, L.
  • Campbell, L.I.
  • Drukewitz, S.H.
  • Undheim, E.A.B.
  • Jenner, R.A.
  • Schiavo, G.
  • Bleidorn, C.
Abstract
    BackgroundWe 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.ResultsOur 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.ConclusionsOur 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.
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