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Using Phage Display to Identify Peptides that Bind to the Surface of Helicobacter pylori Open Access


Other title
Phage display
Heicobacter pylori
Type of item
Degree grantor
University of Alberta
Author or creator
Seetharaman Srinivasan, Praveen Raj
Supervisor and department
Monika Keelan, Laboratory Medicine and Pathology
Examining committee member and department
Jason Acker, Laboratory Medicine and Pathology, Examination Chair
Larry D. Unsworth, Chemical and Materials Engineering
Locksley E. McGann, Laboratory Medicine and Pathology
Leluo Guan, Agriculture, Food and Nutritional Sciences
Medical Sciences- Laboratory Medicine and Pathology

Date accepted
Graduation date
Master of Science
Degree level
Recent studies have reported high rates of Helicobacter pylori (H. pylori) infection and gastric disease in the remote community of Aklavik (NWT) as compared with urban centers in Alberta. Current therapies fail to eradicate 20-25% of H. pylori infections, which may be related to antimicrobial resistance, poor compliance and, perhaps, inadequate drug delivery strategies. Proteins and unknown outer surface molecules (OSM) found on the bacterial surface of H. pylori play a major role in colonization and pathogen-host interaction. A novel therapeutic that will specifically target the OSM of bacteria and kill them may provide an effective alternative for the eradication of H. pylori infections. To this end, it is essential to identify peptides that bind specifically to the OSM of H. pylori. Phage display library is a tool that can interact with OSM of bacteria by exposing a library of a specific phage, each displaying one kind of the PIII minor coat proteins on its surface. This thesis Identified 20 peptides that bind to the OSM of four isolates of H. pylori, which is a first step towards the development of a targeted treatment for H. pylori infection.
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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