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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.


The induction and purification of His-FgTri101 expressed in E. coli BL21(DE3) cells. (a) His-FgTri101 from Fusarium graminearum was induced and overexpressed in BL21(DE3) cells. (b) The enzyme was purified with Clontech’s His-TALON gravity columns by overnight incubation at 4 °C. All washes and subsequent elution steps were conducted at room temperature.
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toxins-08-00261-f001: The induction and purification of His-FgTri101 expressed in E. coli BL21(DE3) cells. (a) His-FgTri101 from Fusarium graminearum was induced and overexpressed in BL21(DE3) cells. (b) The enzyme was purified with Clontech’s His-TALON gravity columns by overnight incubation at 4 °C. All washes and subsequent elution steps were conducted at room temperature.

Mentions: Expression levels of His-tagged FgTri101 in E. coli whole cell lysates are shown in Figure 1a. A clear band of the induced enzyme with the expected molecular weight (52 kDa) was present in the third lane after 0.5 mM IPTG addition overnight.


Beyond Ribosomal Binding: The Increased Polarity and Aberrant Molecular Interactions of 3- epi- deoxynivalenol
The induction and purification of His-FgTri101 expressed in E. coli BL21(DE3) cells. (a) His-FgTri101 from Fusarium graminearum was induced and overexpressed in BL21(DE3) cells. (b) The enzyme was purified with Clontech’s His-TALON gravity columns by overnight incubation at 4 °C. All washes and subsequent elution steps were conducted at room temperature.
© Copyright Policy
Related In: Results  -  Collection

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

toxins-08-00261-f001: The induction and purification of His-FgTri101 expressed in E. coli BL21(DE3) cells. (a) His-FgTri101 from Fusarium graminearum was induced and overexpressed in BL21(DE3) cells. (b) The enzyme was purified with Clontech’s His-TALON gravity columns by overnight incubation at 4 °C. All washes and subsequent elution steps were conducted at room temperature.
Mentions: Expression levels of His-tagged FgTri101 in E. coli whole cell lysates are shown in Figure 1a. A clear band of the induced enzyme with the expected molecular weight (52 kDa) was present in the third lane after 0.5 mM IPTG addition overnight.

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.