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Title: The response of Campylobacter jejuni to pancreatic enzymes
Author: Jowiya, C. W. J.
ISNI:       0000 0004 5362 4992
Awarding Body: University College London (University of London)
Current Institution: University College London (University of London)
Date of Award: 2014
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Campylobacter jejuni is an important food-borne pathogen, and a major cause of bacterial gastroenteritis. Despite this, relatively little is known regarding the way in which C. jejuni colonises hosts, causes disease or survives in the environment during transmission between hosts. C. jejuni responds to a number of biological molecules found in the human intestinal environment such as bile salts leading to the induction of Campylobacter invasion antigens (Cia), and norepinephrine in response to which the bacterium shows increased virulence. In this study we investigated the response of C. jejuni to mammalian pancreatic α-amylase. The results of this study show that C. jejuni responds to pancreatic α-amylase with production of a mucoid colony phenotype that results from increased secretion of extracellular polysaccharide (EPS) identified as an α-dextran, further to this it was found that the amount of extracellular protein produced by C. jejuni was also increased, the proteins where identified using liquid chromatography mass spectrometry (LC-MS), a number of proteins associated with virulence were identified in the samples grown in the presence of α-amylase. In response to pancreatic α-amylase C. jejuni forms significantly increased biofilm and exhibits increased virulence in the Galleria mellonella and Caco-2 epithelial cell models. Furthermore C. jejuni pre exposed to amylase show significantly increased colonisation of chickens and increased resistance to stresses. It is also shown that C. jejuni is able to utilise α-amylase as a nutrient source, this was determined by growing the bacterium on a defined minimal media with the α-amylase as the only source of carbon present. The ability of C. jejuni to respond pancreatic amylase was shown to require proteolytic activity of Cj0511.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available