Barrett, The Honors College at Arizona State University proudly showcases the work of undergraduate honors students by sharing this collection exclusively with the ASU community.

Barrett accepts high performing, academically engaged undergraduate students and works with them in collaboration with all of the other academic units at Arizona State University. All Barrett students complete a thesis or creative project which is an opportunity to explore an intellectual interest and produce an original piece of scholarly research. The thesis or creative project is supervised and defended in front of a faculty committee. Students are able to engage with professors who are nationally recognized in their fields and committed to working with honors students. Completing a Barrett thesis or creative project is an opportunity for undergraduate honors students to contribute to the ASU academic community in a meaningful way.

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Description
A chimeric, humanized monoclonal antibody that recognizes a highly conserved fusion loop found on flaviviruses was constructed with a geminiviral replicon and transiently expressed in Nicotiana benthamiana plants through Agrobacterium tumefaciens infiltration. Characterization and expression studies were then conducted to confirm correct assembly of the antibody. Once the antibody was

A chimeric, humanized monoclonal antibody that recognizes a highly conserved fusion loop found on flaviviruses was constructed with a geminiviral replicon and transiently expressed in Nicotiana benthamiana plants through Agrobacterium tumefaciens infiltration. Characterization and expression studies were then conducted to confirm correct assembly of the antibody. Once the antibody was purified, an ELISA was conducted to validate that the antibody was able to bind to the flavivirus fusion loop.
ContributorsPardhe, Mary (Author) / Mason, Hugh (Thesis director) / Chen, Qiang (Committee member) / Mor, Tsafrir (Committee member) / School of Life Sciences (Contributor) / Department of Information Systems (Contributor) / W.P. Carey School of Business (Contributor) / Barrett, The Honors College (Contributor)
Created2018-05
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Description
Monoclonal antibody therapy focuses on engineering immune cells to target specific peptide sequences indicative of disease. An impediment in the continued advancement of this market is the lack of an efficient, inexpensive means of characterization that can be broadly applied to any antibody while still providing high-density data. Many characterization

Monoclonal antibody therapy focuses on engineering immune cells to target specific peptide sequences indicative of disease. An impediment in the continued advancement of this market is the lack of an efficient, inexpensive means of characterization that can be broadly applied to any antibody while still providing high-density data. Many characterization methods address an antibody's affinity for its cognate sequence but overlook other important aspects of binding behavior such as off-target binding interactions. The purpose of this study is to demonstrate how the binding intensity between an antibody and a library of random-sequence peptides, otherwise known as an immunosignature, can be evaluated to determine antibody specificity and polyreactivity. A total of 24 commercially available monoclonal antibodies were assayed on 125K and 330K peptide microarrays and analyzed using a motif clustering program to predict candidate epitopes within each antigen sequence. The results support the further development of immunosignaturing as an antibody characterization tool that is relevant to both therapeutic and non-therapeutic antibodies.
ContributorsDai, Jennifer T. (Author) / Stafford, Phillip (Thesis director) / Diehnelt, Chris (Committee member) / School of Life Sciences (Contributor) / W.P. Carey School of Business (Contributor) / Barrett, The Honors College (Contributor)
Created2018-05