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Effects of T‐2 toxin on the muscle proteins of shrimp ( Litopenaeus vannamei ) – a proteomics study
Author(s) -
Huang Zhanrui,
Wang Yaling,
Sun Lijun,
Wang Xiaobo,
Lu Pengli,
Liang Guangming,
Pang Huanying,
Wu Qinghua,
Gooneratne Ravi,
Zhao Jian
Publication year - 2019
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.10001
Subject(s) - litopenaeus , shrimp , chemistry , myofibril , gel electrophoresis , proteomics , biochemistry , fish proteins , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , myosin , peptide mass fingerprinting , food science , biology , enzyme , fishery , gene
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). 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 concentration (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. CONCLUSION 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. © 2019 Society of Chemical Industry