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

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.


Changes in DON concentrations in E. coli BL21(DE3) cells overexpressing Fusarium graminearum Tri101. (a) A significant decrease in DON recovery was noted for the construct that encoded for the Tri101 enzyme in comparison to the control or the empty vector. The noted decrease in DON was confirmed to be due to the acetylation of DON by His-FgTri101 (b). The above tendency was observed in two separate experiments, each with three replications, and the different letters signify significant differences between the means according to Fisher’s Least Significant Difference (LSD) test (p < 0.005).
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toxins-08-00261-f003: Changes in DON concentrations in E. coli BL21(DE3) cells overexpressing Fusarium graminearum Tri101. (a) A significant decrease in DON recovery was noted for the construct that encoded for the Tri101 enzyme in comparison to the control or the empty vector. The noted decrease in DON was confirmed to be due to the acetylation of DON by His-FgTri101 (b). The above tendency was observed in two separate experiments, each with three replications, and the different letters signify significant differences between the means according to Fisher’s Least Significant Difference (LSD) test (p < 0.005).

Mentions: In short, FgTri101 was able to interact with DON both in vivo and in vitro as indicated by the C3 carbon acetylation. The in vivo interactions between DON and E. coli BL21(DE3) cells expressing His-FgTri101 led to a significant decrease of DON recovery (Figure 3a) in test tubes in comparison to the tubes that harbored only the LB broth supplemented with 50 µg/mL DON (control) or the empty pET-28a(+) vector (negative control) (Figure 3a).


Beyond Ribosomal Binding: The Increased Polarity and Aberrant Molecular Interactions of 3- epi- deoxynivalenol
Changes in DON concentrations in E. coli BL21(DE3) cells overexpressing Fusarium graminearum Tri101. (a) A significant decrease in DON recovery was noted for the construct that encoded for the Tri101 enzyme in comparison to the control or the empty vector. The noted decrease in DON was confirmed to be due to the acetylation of DON by His-FgTri101 (b). The above tendency was observed in two separate experiments, each with three replications, and the different letters signify significant differences between the means according to Fisher’s Least Significant Difference (LSD) test (p < 0.005).
© Copyright Policy
Related In: Results  -  Collection

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

toxins-08-00261-f003: Changes in DON concentrations in E. coli BL21(DE3) cells overexpressing Fusarium graminearum Tri101. (a) A significant decrease in DON recovery was noted for the construct that encoded for the Tri101 enzyme in comparison to the control or the empty vector. The noted decrease in DON was confirmed to be due to the acetylation of DON by His-FgTri101 (b). The above tendency was observed in two separate experiments, each with three replications, and the different letters signify significant differences between the means according to Fisher’s Least Significant Difference (LSD) test (p < 0.005).
Mentions: In short, FgTri101 was able to interact with DON both in vivo and in vitro as indicated by the C3 carbon acetylation. The in vivo interactions between DON and E. coli BL21(DE3) cells expressing His-FgTri101 led to a significant decrease of DON recovery (Figure 3a) in test tubes in comparison to the tubes that harbored only the LB broth supplemented with 50 µg/mL DON (control) or the empty pET-28a(+) vector (negative control) (Figure 3a).

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.