Beyond Ribosomal Binding: The Increased Polarity and Aberrant Molecular Interactions of 3-epi-deoxynivalenol
Citation
Hassan, Y.I.; Zhu, H.; Zhu, Y.; Zhou, T. Beyond Ribosomal Binding: The Increased Polarity and Aberrant Molecular Interactions of 3-epi-deoxynivalenol. Toxins 2016, 8, 261.
Plain language summary
In this study, we first compare the chromatographic behavior of mycotoxin DON and its biotransformed product 3-epi-DON and later
explore the ability of both compounds to interact with a recombinant encoding Fusarium graminearum Tri101 acetyltransferase enzyme. The research indicated that the increased polarity of 3-epi-DON in addition to its molecular interactions contribute to the overall toxicity reduction of 3-epi-DON.
Abstract
Abstract: Deoxynivalenol (DON) is a secondary fungal metabolite and contaminant mycotoxin that is
widely detected in wheat and corn products cultivated around the world. Bio-remediation methods
have been extensively studied in the past two decades and promising ways to reduce DON-associated
toxicities have been reported. Bacterial epimerization of DON at the C3 carbon was recently reported
to induce a significant loss in the bio-toxicity of the resulting stereoisomer (3-epi-DON) in comparison
to the parental compound, DON. In an earlier study, we confirmed the diminished bio-potency of
3-epi-DON using different mammalian cell lines and mouse models and mechanistically attributed it
to the reduced binding of 3-epi-DON within the ribosomal peptidyl transferase center (PTC). In the
current study and by inspecting the chromatographic behavior of 3-epi-DON and its molecular
interactions with a well-characterized enzyme, Fusarium graminearum Tri101 acetyltransferase, we
provide the evidence that the C3 carbon epimerization of DON influences its molecular interactions
beyond the abrogated PTC binding.