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- Title
Recombinant Aflatoxin-Degrading F420H2-Dependent Reductase from Mycobacterium smegmatis Protects Mammalian Cells from Aflatoxin Toxicity.
- Authors
Li, Che-Hsing; Li, Wei-Yang; Hsu, I-Ning; Yang, Chi-Ya; Chang, Hsiang-Hua; Huang, Ho-Lo; Lo, Shao-Chi; Lin, Ting-Yu; Yang, Yu-Chieh; Liao, Yung-Yu; Taylor, Matthew C.; Liu, Yu-Fan; Huang, Wei-Hao; Sun, Wei-Che; Chuang, Ya-Yi; Fu, Ru-Huei; Tsai, Rong-Tzong
- Abstract
Aflatoxins are carcinogenic secondary metabolites of fungi that contaminate many staple crops and foods. Aflatoxin contamination is a worldwide problem, especially in developing countries, posing health hazards, e.g., causing aflatoxicosis and hepatocellular carcinoma, and even death. Biological solutions for aflatoxin detoxification are environmentally friendly and a cheaper alternative than chemical methods. The aims of the current study were to investigate: (1) the ability of MSMEG_5998, an aflatoxin-degrading F420H2-dependent reductase from Mycobacterium smegmatis, to degrade aflatoxin B1 (AFB1) and reduce AFB1-caused damage in HepG2 cell culture model; and (2) whether a thioredoxin (Trx) linkage of MSMEG_5998 enhanced the enzyme activity. We show that Trx-linked MSMEG_5998 degraded 63% AFB1 and native MSMEG_5998 degraded 31% after 4 h at 22 °C, indicating that the Trx-linked enzyme had a better AFB1-degrading ability. In a HepG2 cell culture model, Trx-linked MSMEG_5998 reduced DNA damage and p53-mediated apoptosis caused by AFB1 to a greater extent than the native enzyme. These findings suggest that Trx-linked MSMEG_5998 could potentially be developed to protect the liver from AFB1 damage, or as a candidate protein to reduce AFB1-related toxicity in animals.
- Subjects
SECONDARY metabolism; AFLATOXINS; THIOREDOXIN; DEAZAFLAVINS; ASPERGILLUS
- Publication
Toxins, 2019, Vol 11, Issue 5, p259
- ISSN
2072-6651
- Publication type
Article
- DOI
10.3390/toxins11050259