Summary and conclusions

Here we present a scheme for describing the life cycle of bacterial protein toxins and a framework for studying the energetics of the conformational changes required for their mode of action. The coupling of structural and molecular biology with thermodynamics allows one to paint a detailed picture of the function of bacterial toxins which can be leveraged to create novel toxins that may be used in crop protection, therapeutic protein discovery, biodefense, biosensor nanotechnology, etc. Figure 1.1 not only describes the key steps in protein toxin function, but also illustrates the complexity required for protein toxins to exert a toxic effect. For a protein to be toxic, or remain toxic in the case of foodborne proteins, not a single step in the toxin life cycle can be negatively impacted. Interruption of the life cycle at any single step can render the protein nontoxic. For example, insecticidal toxins from Bacillus thuringiensis have been shown to be rapidly degraded by simulated human gastric fluid, suggesting that for this toxin the life cycle, if disrupted early in the process, negatively impacts its toxicity.19 This is in contrast to the stability of Bt toxins in insect guts where proteolytic activation of the protein occurs, leading to toxicity to insect cells. This simple example shows how crucial each step in the life cycle of a protein toxin is in determining whether a protein can exhibit its toxic activity, and further highlights the importance of understanding each step of the life cycle in defining the mechanism of action for protein toxins.

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