Document Type

Theses, Masters

Rights

This item is available under a Creative Commons License for non-commercial use only

Disciplines

3.3 HEALTH SCIENCES

Publication Details

Successfully submitted for the award of Master of Philosophy (M.Phil.) to the Dublin Institute of Technology, 2011.

Abstract

Helicobacter pylori is a human pathogen and the causative agent of chronic gastritis, peptic ulcer and gastric malignancies. A number of H. pylori virulence factors have been described including, CagA, VacA, neutrophil activating protein, and expression of receptors for binding to extracellular matrix proteins (adhesins). H. pylori interacts with extracellular matrix (ECM) proteins such as collagen IV, laminin, vitronectin and fibronectin, that can be exposed due to loss of integrity of the gastric epithelial cell layer. These interactions may be important in the pathogenesis of the organism. This study examines the interaction of H. pylori with collagen IV in an attempt to identify a H. pylori collagen IV adhesin. Collagen IV makes up a large proportion of the basement membranes, and has been implicated in microbial adherence. FITC labelling of bacteria and a bacteria overlay method showed binding of H. pylori to ECM proteins collagen IV, laminin and fibronectin. Binding was observed under a variety of culture conditions. Receptor activity-directed tagging known as “Retagging” was employed in an attempt to purify the collagen IV adhesin. H. pylori catalase was identified as a possible collagen adhesin, This enzyme was isolated and its interaction with collagen IV in vitro was studied. However, in vitro binding of collagen IV to catalase could not be demonstrated despite repeated attempts. Immunoblot and receptor overlay techniques were investigated in further attempts to identify the H. pylori collagen IV binding protein. The role of collagen IV in H. pylori ECM binding is discussed.

DOI

10.21427/D72317

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Food Science Commons

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