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Full-Text Articles in Immunology of Infectious Disease
Mechanisms By Which Protective Human Outer Surface Protein A Antibodies Block Transmission Of Borrelia Burgdorferi, Amber M. Frye
Mechanisms By Which Protective Human Outer Surface Protein A Antibodies Block Transmission Of Borrelia Burgdorferi, Amber M. Frye
Legacy Theses & Dissertations (2009 - 2024)
Borrelia burgdorferi (B. burgdorferi) is the causative agent of Lyme disease in the United States and Europe, which remains a major threat to public health. While currently no human Lyme disease vaccine is available, a previously licensed OspA-based vaccine was shown to effectively prevent transmission of B. burgdorferi from ticks to mammalian hosts. Concerning the vaccines mechanism of action, OspA antibodies enter the bloodmeal of a feeding tick and engage with B. burgdorferi producing OspA on their outer surface in a manner that impairs migration of the spirochete to the host; however exact antibody-spirochete interaction is unknown, despite the importance …
Assessing The Durability Of The Immune Response Induced By Rivax®, A Ricin Subunit Vaccine, Hayley Lynn Novak
Assessing The Durability Of The Immune Response Induced By Rivax®, A Ricin Subunit Vaccine, Hayley Lynn Novak
Legacy Theses & Dissertations (2009 - 2024)
Assessing the performance and durability of the antibody response in animal models can assist in the development of biodefense vaccines. Ricin is one of the most toxic biological agents known and has been a public health issue for years. Since ricin is easily manufactured and a deadly toxin, rational vaccine design and immunotherapeutic optimization have been explored. RiVax® is a candidate subunit vaccine with a modified A-chain of ricin toxin that was formulated to remove ricin's biological activity. It is thought that RiVax® could serve as a prophylactic that would induce humoral- and cell-mediated immunological responses that elicit protective antigens …
Intrabodies Reveal Critical Steps Involved In Ricin's Interactions With The Ribosome, Timothy Francis Czajka
Intrabodies Reveal Critical Steps Involved In Ricin's Interactions With The Ribosome, Timothy Francis Czajka
Legacy Theses & Dissertations (2009 - 2024)
Ricin is a highly lethal protein toxin derived from the seeds of the castor plant, Ricinus communis. It is a Type II ribosome inactivating protein (RIP), meaning it is a heterodimer with one subunit, ricin toxin B (RTB), that mediates cell surface attachment and intracellular trafficking and a second subunit, ricin toxin A (RTA), that irreversibly shuts down protein synthesis in the cytosol. During trafficking, RTA and RTB necessarily separate in the endoplasmic reticulum, wherein RTA unfolds and translocates into the cytosol where it refolds into an enzymatically active conformation. RTA is remarkably fast acting and efficient, with few molecules …
Role Of Antibody Isotypes In Providing Passive Protection Against Ricin Toxin, Ipneet Kaur Dhaliwal
Role Of Antibody Isotypes In Providing Passive Protection Against Ricin Toxin, Ipneet Kaur Dhaliwal
Legacy Theses & Dissertations (2009 - 2024)
Ricin toxin is a glycoprotein produced by the castor bean plant, Ricinus communis. Ricin is an extraordinarily potent inducer of cell death and inflammation, especially following inhalation. The toxin’s enzymatic subunit (RTA) is transported via retrograde transport into the cytoplasm of mammalian cells by the toxin’s B subunit (RTB). Once in the cytoplasm, RTA inactivates ribosomes through cleavage of ribosomal RNA. In this study, I characterized a ricin-specific monoclonal IgA antibody (mAb) known as 23D7. I confirmed that 23D7 reacts with RTA and is effective at neutralizing ricin in a Vero cell cytotoxicity assay in vitro. To localize the epitope …
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 …