Date of Award

1-1-2020

Language

English

Document Type

Dissertation

Degree Name

Doctor of Philosophy (PhD)

College/School/Department

Department of Biomedical Sciences

Content Description

1 online resource (xxi, 249 pages) : color illustrations.

Dissertation/Thesis Chair

Nicholas J Mantis

Committee Members

Janice D Pata, Christina Egan, Michael J Rudolph, Robert Linhardt, Kathleen A McDonough

Keywords

antibody, epitope, neutralizing, ricin, Ricin, Apoptosis, Immunoglobulins

Subject Categories

Biology

Abstract

Ricin is a member of the ribosome-inactivating protein (RIP) family of toxins found throughout the plant and microbial worlds. In its mature form, ricin is a 65 kDa glycoprotein consisting of two subunits, RTA and RTB, joined by a single disulfide bond. RTA (267 amino acids) is an RNA N-glycosidase that mediates the depurination of a universally conserved residue within the Sarcin-ricin loop (SRL) ribosomal RNA element. RTB is a galactose-/N-acetylgalactosamine-specific lectin that facilitates attachment, endocytosis, and intracellular trafficking of ricin in mammalian cells. Following endocytosis, ricin is routed to the trans-Golgi network (TGN) and then shuttled to the endoplasmic reticulum (ER), where RTA is liberated from RTB. RTA is then translocated into the cytosol where it targets ribosomes.

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