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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2017
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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. |
format | Online Article Text |
id | pubmed-5535152 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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