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Mar. Drugs 2017, 15(1), 21; doi:10.3390/md15010021

Molecular Characterization of Voltage-Gated Sodium Channels and Their Relations with Paralytic Shellfish Toxin Bioaccumulation in the Pacific Oyster Crassostrea gigas

1
Laboratoire des Sciences de l’Environnement Marin (LEMAR), Institut Universitaire Européen de la Mer, Université de Bretagne Occidentale, UMR 6539 CNRS/UBO/IRD/Ifremer, 29280 Plouzané, France
2
Laboratory of Immunology and Pathology of Invertebrates, Department of Molecular Biology, Exact and Natural Sciences Center, Federal University of Paraíba—Campus I, 58051-900 João Pessoa, PB, Brazil
3
UMR 5805 EPOC, CNRS—Équipe Écotoxicologie Aquatique, Université de Bordeaux, Station Marine d’Arcachon, 33120 Arcachon, France
4
Laboratoire Phycotoxines, IFREMER, BP 21105, 44311 Nantes, France
5
Ifremer, UMR 6539 LEMAR CNRS/UBO/IRD/Ifremer, 29280 Plouzané, France
*
Authors to whom correspondence should be addressed.
Academic Editor: Lucio Costa
Received: 16 November 2016 / Revised: 4 January 2017 / Accepted: 6 January 2017 / Published: 19 January 2017
(This article belongs to the Special Issue Marine Neurotoxins)
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Abstract

Paralytic shellfish toxins (PST) bind to voltage-gated sodium channels (Nav) and block conduction of action potential in excitable cells. This study aimed to (i) characterize Nav sequences in Crassostrea gigas and (ii) investigate a putative relation between Nav and PST-bioaccumulation in oysters. The phylogenetic analysis highlighted two types of Nav in C. gigas: a Nav1 (CgNav1) and a Nav2 (CgNav2) with sequence properties of sodium-selective and sodium/calcium-selective channels, respectively. Three alternative splice transcripts of CgNav1 named A, B and C, were characterized. The expression of CgNav1, analyzed by in situ hybridization, is specific to nervous cells and to structures corresponding to neuromuscular junctions. Real-time PCR analyses showed a strong expression of CgNav1A in the striated muscle while CgNav1B is mainly expressed in visceral ganglia. CgNav1C expression is ubiquitous. The PST binding site (domain II) of CgNav1 variants possess an amino acid Q that could potentially confer a partial saxitoxin (STX)-resistance to the channel. The CgNav1 genotype or alternative splicing would not be the key point determining PST bioaccumulation level in oysters. View Full-Text
Keywords: Crassostrea gigas; sodium channel; alternative splicing; Alexandrium minutum; paralytic shellfish toxins Crassostrea gigas; sodium channel; alternative splicing; Alexandrium minutum; paralytic shellfish toxins
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Boullot, F.; Castrec, J.; Bidault, A.; Dantas, N.; Payton, L.; Perrigault, M.; Tran, D.; Amzil, Z.; Boudry, P.; Soudant, P.; Hégaret, H.; Fabioux, C. Molecular Characterization of Voltage-Gated Sodium Channels and Their Relations with Paralytic Shellfish Toxin Bioaccumulation in the Pacific Oyster Crassostrea gigas. Mar. Drugs 2017, 15, 21.

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