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Beyond Ribosomal Binding: The Increased Polarity and Aberrant Molecular Interactions of 3- epi- deoxynivalenol

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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.

No MeSH data available.


Related in: MedlinePlus

Both DON and 3-epi-DON interacted with the same conjugated commercial DON-monoclonal antibody in a similar fashion. The chromatographic separation of DON and 3-epi-DON after the affinity column purification step (DONtest) and injection on Jupiter 4µ Proteo 90A HPLC column is shown. The results indicated that DON (a) was captured in a similar fashion to 3-epi-DON (b).
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toxins-08-00261-f005: Both DON and 3-epi-DON interacted with the same conjugated commercial DON-monoclonal antibody in a similar fashion. The chromatographic separation of DON and 3-epi-DON after the affinity column purification step (DONtest) and injection on Jupiter 4µ Proteo 90A HPLC column is shown. The results indicated that DON (a) was captured in a similar fashion to 3-epi-DON (b).

Mentions: Satisfyingly enough, the DONtest immunoaffinity column showed the ability to bind 3-epi-DON in a comparable fashion to DON. When the methanol eluted compounds were analyzed using HPLC methods described below, both metabolites were detectable as indicated in Figure 5.


Beyond Ribosomal Binding: The Increased Polarity and Aberrant Molecular Interactions of 3- epi- deoxynivalenol
Both DON and 3-epi-DON interacted with the same conjugated commercial DON-monoclonal antibody in a similar fashion. The chromatographic separation of DON and 3-epi-DON after the affinity column purification step (DONtest) and injection on Jupiter 4µ Proteo 90A HPLC column is shown. The results indicated that DON (a) was captured in a similar fashion to 3-epi-DON (b).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC5037487&req=5

toxins-08-00261-f005: Both DON and 3-epi-DON interacted with the same conjugated commercial DON-monoclonal antibody in a similar fashion. The chromatographic separation of DON and 3-epi-DON after the affinity column purification step (DONtest) and injection on Jupiter 4µ Proteo 90A HPLC column is shown. The results indicated that DON (a) was captured in a similar fashion to 3-epi-DON (b).
Mentions: Satisfyingly enough, the DONtest immunoaffinity column showed the ability to bind 3-epi-DON in a comparable fashion to DON. When the methanol eluted compounds were analyzed using HPLC methods described below, both metabolites were detectable as indicated in Figure 5.

View Article: PubMed Central - PubMed

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.

No MeSH data available.


Related in: MedlinePlus