You are here

UCF Digital Collections ยป Honors Collection

IDENTIFICATION OF THE DOMAIN(S) IN PROTEIN DISULFIDE ISOMERASE REQUIRED FOR BINDING AND DISASSEMBLY OF THE CHOLERA HOLOTOXIN

Download pdf | Full Screen View

Date Issued:
2015
Abstract/Description:
Cholera, caused by the secretion of cholera toxin (CT) by Vibrio cholerae within the intestinal lumen, triggers massive secretory diarrhea which may lead to life-threatening dehydration. CT is an AB5-type protein toxin that is comprised of an enzymatically active A1 chain, an A2 linker, and a cell-binding B pentamer. Once secreted, the CT holotoxin moves from the cell surface to the endoplasmic reticulum (ER) of a host target cell. To cause intoxication, CTA1 must be displaced from CTA2/CTB5 in the ER and is then transferred to the cytosol where it induces a diarrheal response by stimulating the efflux of chloride ions into the intestinal lumen. Protein disulfide isomerase (PDI), a resident ER oxidoreductase and chaperone, is involved in detaching CTA1 from the holotoxin. The PDI domain(s) that binds to CTA1 and precisely how this interaction is involved in CTA1 dissociation from the holotoxin are unknown. The goal of this project is to identify which domain(s) of PDI is responsible for binding to and dislodging CTA1 from the CT holotoxin. Through incorporation of ELISA, surface plasmon resonance (SPR), and Fourier transform infrared (FTIR) spectroscopy techniques in conjunction with a panel of purified PDI deletion constructs, this project aims to provide important molecular insight into a crucial interaction of the CT intoxication process.
Title: IDENTIFICATION OF THE DOMAIN(S) IN PROTEIN DISULFIDE ISOMERASE REQUIRED FOR BINDING AND DISASSEMBLY OF THE CHOLERA HOLOTOXIN.
30 views
14 downloads
Name(s): Herndon, Laura, Author
Teter, Ken, Committee Chair
University of Central Florida, Degree Grantor
Type of Resource: text
Date Issued: 2015
Publisher: University of Central Florida
Language(s): English
Abstract/Description: Cholera, caused by the secretion of cholera toxin (CT) by Vibrio cholerae within the intestinal lumen, triggers massive secretory diarrhea which may lead to life-threatening dehydration. CT is an AB5-type protein toxin that is comprised of an enzymatically active A1 chain, an A2 linker, and a cell-binding B pentamer. Once secreted, the CT holotoxin moves from the cell surface to the endoplasmic reticulum (ER) of a host target cell. To cause intoxication, CTA1 must be displaced from CTA2/CTB5 in the ER and is then transferred to the cytosol where it induces a diarrheal response by stimulating the efflux of chloride ions into the intestinal lumen. Protein disulfide isomerase (PDI), a resident ER oxidoreductase and chaperone, is involved in detaching CTA1 from the holotoxin. The PDI domain(s) that binds to CTA1 and precisely how this interaction is involved in CTA1 dissociation from the holotoxin are unknown. The goal of this project is to identify which domain(s) of PDI is responsible for binding to and dislodging CTA1 from the CT holotoxin. Through incorporation of ELISA, surface plasmon resonance (SPR), and Fourier transform infrared (FTIR) spectroscopy techniques in conjunction with a panel of purified PDI deletion constructs, this project aims to provide important molecular insight into a crucial interaction of the CT intoxication process.
Identifier: CFH0004792 (IID), ucf:45334 (fedora)
Note(s): 2015-05-01
B.S.
Medicine, Burnett School of Biomedical Sciences
Bachelors
This record was generated from author submitted information.
Subject(s): cholera
cholera toxin
protein disulfide isomerase
Persistent Link to This Record: http://purl.flvc.org/ucf/fd/CFH0004792
Restrictions on Access: campus 2018-04-01
Host Institution: UCF

In Collections