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Biooxidation of Ciguatoxins Leads to Species-Specific Toxin Profiles

Ciguatoxins (CTXs) contaminate fish worldwide and cause the foodborne illness ciguatera. In the Pacific, these toxins are produced by the dinoflagellate Gambierdiscus toxicus, which accumulates in fish through the food chain and undergoes oxidative modification, giving rise to numerous analogs. In t...

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Autores principales: Ikehara, Tsuyoshi, Kuniyoshi, Kyoko, Oshiro, Naomasa, Yasumoto, Takeshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5535152/
https://www.ncbi.nlm.nih.gov/pubmed/28661447
http://dx.doi.org/10.3390/toxins9070205
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author Ikehara, Tsuyoshi
Kuniyoshi, Kyoko
Oshiro, Naomasa
Yasumoto, Takeshi
author_facet Ikehara, Tsuyoshi
Kuniyoshi, Kyoko
Oshiro, Naomasa
Yasumoto, Takeshi
author_sort Ikehara, Tsuyoshi
collection PubMed
description Ciguatoxins (CTXs) contaminate fish worldwide and cause the foodborne illness ciguatera. In the Pacific, these toxins are produced by the dinoflagellate Gambierdiscus toxicus, which accumulates in fish through the food chain and undergoes oxidative modification, giving rise to numerous analogs. In this study, we examined the oxidation of CTXs in vitro with liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis using reference toxins, and found that CTX4A, CTX4B, and CTX3C, which are produced by the alga, are oxidized to the analogs found in fish, namely CTX1B, 52-epi-54-deoxyCTX1B, 54-deoxyCTX1B, 2-hydroxyCTX3C, and 2,3-dihydroxyCTX3C. This oxidation was catalyzed by human CYP3A4, fish liver S9 fractions, and microsomal fractions prepared from representative ciguateric fishes (Lutjanus bohar, L. monostigumus, and Oplegnathus punctatus). In addition, fish liver S9 fractions prepared from non-ciguateric fishes (L. gibbus and L. fulviflamma) in Okinawa also converted CTX4A and CTX4B to CTX1B, 54-deoxyCTX1B, and 52-epi-54-deoxyCTX1B in vitro. This is the first study to demonstrate the enzymatic oxidation of these toxins, and provides insight into the mechanism underlying the development of species-specific toxin profiles and the fate of these toxins in humans and fish.
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spelling pubmed-55351522017-08-04 Biooxidation of Ciguatoxins Leads to Species-Specific Toxin Profiles Ikehara, Tsuyoshi Kuniyoshi, Kyoko Oshiro, Naomasa Yasumoto, Takeshi Toxins (Basel) Article Ciguatoxins (CTXs) contaminate fish worldwide and cause the foodborne illness ciguatera. In the Pacific, these toxins are produced by the dinoflagellate Gambierdiscus toxicus, which accumulates in fish through the food chain and undergoes oxidative modification, giving rise to numerous analogs. In this study, we examined the oxidation of CTXs in vitro with liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis using reference toxins, and found that CTX4A, CTX4B, and CTX3C, which are produced by the alga, are oxidized to the analogs found in fish, namely CTX1B, 52-epi-54-deoxyCTX1B, 54-deoxyCTX1B, 2-hydroxyCTX3C, and 2,3-dihydroxyCTX3C. This oxidation was catalyzed by human CYP3A4, fish liver S9 fractions, and microsomal fractions prepared from representative ciguateric fishes (Lutjanus bohar, L. monostigumus, and Oplegnathus punctatus). In addition, fish liver S9 fractions prepared from non-ciguateric fishes (L. gibbus and L. fulviflamma) in Okinawa also converted CTX4A and CTX4B to CTX1B, 54-deoxyCTX1B, and 52-epi-54-deoxyCTX1B in vitro. This is the first study to demonstrate the enzymatic oxidation of these toxins, and provides insight into the mechanism underlying the development of species-specific toxin profiles and the fate of these toxins in humans and fish. MDPI 2017-06-29 /pmc/articles/PMC5535152/ /pubmed/28661447 http://dx.doi.org/10.3390/toxins9070205 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Ikehara, Tsuyoshi
Kuniyoshi, Kyoko
Oshiro, Naomasa
Yasumoto, Takeshi
Biooxidation of Ciguatoxins Leads to Species-Specific Toxin Profiles
title Biooxidation of Ciguatoxins Leads to Species-Specific Toxin Profiles
title_full Biooxidation of Ciguatoxins Leads to Species-Specific Toxin Profiles
title_fullStr Biooxidation of Ciguatoxins Leads to Species-Specific Toxin Profiles
title_full_unstemmed Biooxidation of Ciguatoxins Leads to Species-Specific Toxin Profiles
title_short Biooxidation of Ciguatoxins Leads to Species-Specific Toxin Profiles
title_sort biooxidation of ciguatoxins leads to species-specific toxin profiles
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5535152/
https://www.ncbi.nlm.nih.gov/pubmed/28661447
http://dx.doi.org/10.3390/toxins9070205
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