My choice to take part in current work with bacterial toxins was driven by my interest in bacterial pathogens and public health. It was the infectious nature and deadly illnesses of pathogenic bacteria that drove me to study microbiology, but my time at the University of Illinois has revealed a whole new world of utility and beneficial applications that we can garner from our microscopic friends. I hope to continue studying pathogenic mechanisms of bacteria in the future at an academic or public health research institution. I am also interested in working to improve public education and relations on scientific matters.
Bacterial AB type protein toxins are comprised of functional domains for cell binding, translocation into the host cytosol, and catalytic activity. Cytotoxic necrotizing factor (CNF) toxins enter the host cell through receptor-mediated endocytosis and translocate their catalytic domain in a pH-dependent manner into the host cell cytosol where they deamidate Rho-like GTPases resulting in constitutive activation. Here, we swapped functional domains of homologous CNF toxins and observed the effect on the resulting chimeras to efficiently deliver their toxic cargo into the host cell cytosol. We assess whether the CNF functional domains are indiscriminately interchangeable or if the domains are co-dependent. Results from this study provide insights into the protein determinants that define toxin-based delivery of toxic cargo, which will contribute to improving the intelligent design of recombinant toxin-based delivery vehicles for clinical and research applications.