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Identification Of Epitopes On Ricin Toxin's Enzymatic Subunit (Rta) Critical For Eliciting Neutralizing Antibodies And Protective Immunity, Joanne Marie O'Hara
Identification Of Epitopes On Ricin Toxin's Enzymatic Subunit (Rta) Critical For Eliciting Neutralizing Antibodies And Protective Immunity, Joanne Marie O'Hara
Legacy Theses & Dissertations (2009 - 2024)
Ricin toxin's enzymatic subunit (RTA) is a 267 amino acid RNA N-glycosidase that selectively depurinates eukaryotic ribosomal RNA and arrests protein synthesis. The crystal structure of RTA revealed that the protein assumes three distinct folding domains (FD). Residues within FD1 and FD2 form RTA's active site pocket and are proposed to interface with ribosomal proteins, while FD3's primary function is to associate with ricin's B subunit (RTB). In this study I sought to identify the regions of RTA that are important in eliciting toxin-neutralizing antibodies (TNA), as this information is critical for current efforts to develop RTA-based subunit vaccines. I …
The Role Of Pkr In Transducing The Ribotoxic Stress Response Elicited By Ricin, Lauren Rose-Boehnlein
The Role Of Pkr In Transducing The Ribotoxic Stress Response Elicited By Ricin, Lauren Rose-Boehnlein
Legacy Theses & Dissertations (2009 - 2024)
Ribotoxins such as ricin and T-2 toxin bind to ribosomes and trigger cleavage of 28S rRNA and inhibition of protein synthesis. Upon detection of ribosomal alterations, the cell initiates a ribotoxic stress response (RSR), resulting in activation of the stress-activated protein kinase and mitogen-activated protein kinase (SAPK/MAPK) signaling cascade, upregulated expression of both pro-and anti-apoptotic stress-inducible genes, increased secretion of inflammatory cytokines, and ultimately culminating in apoptosis. While it is not immediately clear the exact mechanism by which ribosomes induce the RSR, nor the exact cellular components involved upstream of MAPK activation, it has recently been proposed, in the case …