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BACKGROUND: T-2 toxin (T-2) is a potent mycotoxin and a common contaminant of aquatic animal feed, posing a serious risk to health and aquatic animals. We investigated the effect of T-2 on shrimp muscle proteins using proteomics and conventional biochemical methods. Shrimp were fed a diet containing T-2 at 0-12.2 mg kg −1 for 20 days, and changes to the muscle protein composition, ATPase activities, and the sulfhydryl (SH) content and hydrophobicity of actomyosin (AM) were determined. A proteomics study of the proteins was conducted with sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), two-dimensional (2D) electrophoresis, and matrix-assisted laser desorption/ionization -time of flight mass spectrometry (MALDI-TOF/TOF MS). (1.2 mg kg −1 ), the levels of three major muscle proteins (myofibrillar, sarcoplasmic, and stroma) increased but at higher concentrations they declined progressively. T-2 exposure also led to a breakdown of muscle proteins as evidenced by increases in alkali-soluble protein and the surface hydrophobicity (SoANS) of AM. Thirty differentially expressed proteins were detected, 12 of which showed a concentration-response relationship with T-2 exposure. Among them, 11 homologous proteins were identified by mass spectrometry (MS), with several being key enzymes in energy metabolism. RESULTS: Exposure to T-2 markedly affected the muscle protein composition of shrimp in a concentration-responsive manner that displayed a diphasic effect. At a low T-2 concentrationCONCLUSION: This study demonstrated that T-2 exposure at medium to high concentrations could significantly affect the protein composition and quality of shrimp muscle, and potentially some of its key metabolisms. One of the arginine kinases (spot 27) was particularly responsive to T-2 and could potentially be used as a biomarker protein for T-2 intoxication by shrimp. /jsfa dine muscle stored at 0 ∘ C. J Food Sci 65:40-47 (2000).30 Tsuchiya T, Tsuchiya Y, Nonomura Y and Matsumoto JJ, Prevention of freeze denaturation of carp actomyosin by sodium glutamate.

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T-2 toxin (T-2) is a type-A trichothecene produced by Fusarium that causes toxicity to animals. T-2 contamination of grain-based aquatic feed is a concern for the industries related to edible aquatic crustacean species such as the shrimp industry because it can lead to serious food safety issues. T-2, its metabolites, and selected phase I (EROD, CarE) and phase II (GST, UGT, SULT) detoxification enzymes in hemolymph and tissues were monitored at 0, 5, 10 15, 30, 45, and 60 min following T-2 intramuscular administration (3 mg/kg bw) in shrimp (Litopenaeus vannamei). Marked increases of EROD activity in hepatopancreas and CarE activity in hemolymph, gill, hepatopancreas and intestine were observed followed by increases in phase II enzymes (GST, UGT, SULT) in hepatopancreas, hemolymph, intestine and gill, which remained elevated for an extended period. Time-dependent decrease in shrimp tissue T-2 concentration was observed. HT-2 increased up to 15 min. Most other T-2 metabolites were detected but not T-2 tetraol. Enzyme responses on exposure to T-2 were tissue-specific and time-dependent. Detection results indicated that HT-2 may not be the only important metabolite in aquatic crustacean species. Further investigation into T-2 metabolite toxicity is needed to fully understand the food safety issues related to T-2.

We report the artificial synthesis from T-2 toxin of a type A trichothecenes complete antigen. First, 3-AcT -2 was made from T-2 following acetylation. Then 3-Ac-NEOS as a T-2 skeleton structure was synthesized by enzymolysis and identified by liquid chromatography-tandem mass spectrometry and nuclear magnetic resonance. Next, a hapten (3-Ac-NEOS-HS) was formed by modifying the C8 position of 3-Ac-NEOS using succinic anhydride method. 3-Ac-NEOS-HS-BSA/-OVA were prepared by conjugating hapten with bovine serum albumin (BSA) or ovalbumin (OVA) by carbodiimide method and identified by UV spectroscopy and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Results showed that conjugation ratio of 3-Ac-NEOS-HS to BSA was 8.76: 1 and OVA 7.24: 1, indicating 3-Ac-NEOS-HS-BSA as a complete antigen was better. Next we used it to immunize rabbits and obtained a 1:64,000 antibody titre. In conclusion, a type A trichothecenes complete antigen was successfully synthesized, which was the foundation for antibody preparation and enzyme-linked immunosorbent assay kit development for all type A trichothecenes (parent + modified/ masked type A trichothecenes).