Origins of ciguatera fish poisoning: a new dinoflagellate, Gambierdiscus toxicus Adachi and Fukuyo, definitively involved as a causal agent

Bagnis, R.; Chanteau, Suzanne; Chungue, Eliane; Hurtel, J.M.; Yasumoto, Takeshi; Inoue, Akio

doi:10.1016/0041-0101(80)90074-4

Cited by 201 publications

(87 citation statements)

References 8 publications

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“…Ciguatoxins are biosynthesized by the dinoflagellate Gambierdiscus toxicus [1,2], accumulate in tropical fish, and can cause seafood poisoning known as ''ciguatera'' [3]. Many people are poisoned by ciguatoxins in tropical and subtropical seacoast areas [4], and the poisonings are occasionally fatal [5].…”

Section: Introductionmentioning

confidence: 99%

A study on mechanisms of toxic actions of ciguatoxins: existence of functional relationship between CTX3C and charged residues of voltage sensors in Nav1.4 sodium channel

2011

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Ciguatoxins, a group of virulent marine toxins, are bound to ''site 5'' inside voltage-dependent sodium channels and alter their kinetics dramatically; this is probably responsible for clinical symptoms of ciguatoxin poisoning or ciguatera. Although ciguatoxins are known to affect the voltage dependency of both activation and inactivation kinetics, site 5 has not been functionally clarified. This study, therefore, targeted putative voltage sensors as a receptor for ciguatoxins. We constructed mutants, in which 1 of 23 basic residues was substituted with glutamine in the S4 segment for each of four domains. We then examined the effects of a synthetic ciguatoxin congener CTX3C on these mutants. Notably, the suppressive effect of CTX3C on the sodium current (I Na ) amplitude of domain 2 mutants, which carried a mutation in the basic S4 residue of domain 2, was either reduced or eliminated. Kinetic analyses of domain 2 mutants in comparison with those of the wild type and other mutants revealed that the negative shift of the steady-state inactivation curve (V 1/2inact D) was significantly decreased. The resistance of domain 2 mutants to CTX3C in terms of changes in V 1/2inact is suggested to be closely related to resistance to the suppressive effect of CTX3C on the I Na amplitude. This is the first report to demonstrate the existence of a functional relationship between a ciguatoxin congener and voltage sensor segments in domain 2 of the a-subunit of voltage-dependent sodium channels, although further studies are needed to locate a ciguatoxin receptor.

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Section: Introductionmentioning

confidence: 99%

A study on mechanisms of toxic actions of ciguatoxins: existence of functional relationship between CTX3C and charged residues of voltage sensors in Nav1.4 sodium channel

2011

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“…2). In addition to G. toxicus (Adachi and Fukuyo 1979), the first species implicated in ciguatoxin production in biodetritus (Yasumoto et al 1977;Bagnis et al 1980) and monoalgal cultures (Bagnis et al 1980;Holmes et al 1991), other Gambierdiscus spp. with the potential to biosynthesize ciguatoxin now include G. polynesiensis, G. belizeanus, G. australes, G. caribbaeus, G. carolinianus, G. carpenteri, and G. ruetzleri (Chinain et al 1999;Litaker et al 2009).…”

Section: Origin and Transfer Of Ciguatoxins To Fishmentioning

confidence: 99%

Ciguatoxin and Ciguatera

Lewis

Vetter

2016

Marine and Freshwater Toxins

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“…Ciguatera (CTX), first isolated from a dinoflagellate from the Gambier Islands and termed Gambierdiscus toxicus [11], is the most common nonbacterial food toxin related to seafood ingestion in the US, Canada, and, more recently, Europe, and represents one of the most intriguing toxins from several perspectives. CTX is a serious although rarely lethal human food toxin related to the consumption of tropical reef fish.…”

Section: Ciguateramentioning

confidence: 99%