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Characterizing And Epitope Mapping Single-Domain Antibodies On Borrelia Burgdorferi Protein Ospa, Saiful Basir
Characterizing And Epitope Mapping Single-Domain Antibodies On Borrelia Burgdorferi Protein Ospa, Saiful Basir
Legacy Theses & Dissertations (2009 - 2024)
Epitope mapping a protein that enables pathogenesis is crucial for the development of therapies and prophylactics that can inhibit the pathogen’s function and its transmission of disease. The lipoprotein OspA enables Lyme Disease etiologic pathogen, Borrelia burgdorferi, to inhabit the tick midgut until transmission occurs. Anti-OspA mAbs and their smaller VHH counterparts are highly specific and tailored to bind proteins such as OspA, reproducibly, at established binding sites or epitopes. Previous studies found an array of mAbs that successfully bound OspA and have already been used in epitope mapping. To our knowledge, this is the first use of VHHs in …
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 …
Identification Of B-Cell Epitopes On Domain 4 Of Anthrax Protective Antigen, Cassandra D. Kelly-Cirino
Identification Of B-Cell Epitopes On Domain 4 Of Anthrax Protective Antigen, Cassandra D. Kelly-Cirino
Legacy Theses & Dissertations (2009 - 2024)
Protective Antigen (PA) is the receptor binding subunit common to both Lethal (LT) and Edema (ET) toxins, which contribute to the mortality associated with Bacillus anthracis infection. While recombinant PA (rPA) is likely to be an important constituent of second generation anthrax vaccines, evaluating the effectiveness of candidate vaccines is currently difficult, because the specific B cell epitopes involved in toxin neutralization have not been completely defined. The only well characterized antibody, 14B7, has been shown to disrupt the association of PA with the anthrax toxin receptors (ATR) by binding to domain 4 of PA. I hypothesized that other domain …