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Abstract
The interaction between the Shiga toxin B-subunit (STxB) and its globotriaosylceramide receptor (Gb3) has a high potential for being exploited for targeted cancer therapy. The primary goal of this study was to evaluate the capacity of STxB to carry small molecules and proteins as cargo into cells. For this purpose, an assay was designed to provide real-time information about the StxB-Gb3 interaction as well as the dynamics and mechanism of the internalization process. The assay revealed the ability to distinguish the process of binding to the cell surface from internalization and presented the importance of receptor and STxB clustering for internalization. The overall setup demonstrated that the binding mechanism is complex, and the concept of affinity is difficult to apply. Hence, time-resolved methods, providing detailed information about the interaction of STxB with cells, are critical for the optimization of intracellular delivery.
Highlights
The interaction between the Shiga toxin B-subunit (STxB) and its globotriaosylceramide receptor (Gb3) has a high potential for being exploited for targeted cancer therapy
Discovering vectors that bind to cell surface molecules that are specific for, or overproduced by, cancer cells enables the design of therapies that target cancer with higher specificity [2]
To evaluate how Shiga toxin subunit B (STxB) was affected by fluorescein isothiocyanate (FITC)-labeling, a thermal shift analysis monitoring the intrinsic fluorescence at 330 and 350 nm from 35 °C to 95 °C was performed
Summary
The interaction between the Shiga toxin B-subunit (STxB) and its globotriaosylceramide receptor (Gb3) has a high potential for being exploited for targeted cancer therapy. The primary goal of this study was to evaluate the capacity of STxB to carry small molecules and proteins as cargo into cells For this purpose, an assay was designed to provide real-time information about the StxB–Gb3 interaction as well as the dynamics and mechanism of the internalization process. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies Real-time analysis of binding and internalization of STxB these drugs has been reported, caused by mechanisms such as impaired lysosomal function or antigen-related resistance [4]
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