Date of Award

1-1-2023

Language

English

Document Type

Master's Thesis

Degree Name

Master of Science (MS)

College/School/Department

Department of Biomedical Sciences

Content Description

1 online resource (vi, 63 pages) : illustrations (some color)

Dissertation/Thesis Chair

Nicholas Mantis

Committee Members

Janice Pata, Douglas Conklin

Keywords

Immunoglobulins, Ribosomes

Subject Categories

Biology

Abstract

Assessing the ability of VHHs to protect ribosomes from the depurination activity of Ricin toxin’s(RT) enzymatic subunit, RTA, can provide insights regarding binding placement, epitopes of interest and role of affinity in neutralization is critical for the development of anti-toxin countermeasures. Determining the level of correlation between binding strength, binding location and elicited protection can be useful for future and ongoing research. Ricin is easily manufactured and considered one of the most toxic biological agents known. Without an approved vaccine, continued research to design and optimize therapeutic countermeasures is essential. Over the past decade single-domain antibodies (VHHs) have been recognized for their therapeutic potential against various emerging infectious diseases and biological threats. In this report we have characterized four of these VHHs for their potential to bind RT and ability to inhibit RTA’s enzymatic activity in an in vitro assay. One of the VHHs, V5C1 is a moderate inhibitor of RTA activity.

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