Helicobacter pylori infects and colonises in the human gastric where the infection can lead to gastric diseases. There are also a number of other Helicobacter species referred to as non-pylori Helicobacters that colonise other parts of the gastrointestinal tract. To understand those characteristics of the non-pylori Helicobacters that allow them to colonise different sites in the body resulting in different patterns of infection, the analysis of Helicobacter pylori and non-pylori Helicobacter proteomes was initiated. Total cellular proteins were extracted and compared using 2-DE. The Helicobacter proteome showed a high level of variability between different H. pylori strains as well as between the eight Helicobacter species analysed. It was proposed that some of the proteomic variation related to the pathogenic potential of the bacteria. Differential syntheses of specific proteins were found to be associated with H. pylori isolates associated with two different disease outcomes. Differential patterns of protein synthesis were also observed to discriminate between the Helicobacter isolates according to their site of colonisation defined as gastric and enterohepatic Helicobacter groups. Significant protein spots were identified by peptide fragment fingerprinting and LC-MS/MS. To provide additional functional information on the bacterial proteins, the Helicobacter hydrophobic proteins, which are typically located in the bacterial membrane and may be involved in bacterial host interactions, were analysed. Triton X-114 was used to enrich the bacterial hydrophilic and hydrophobic proteins which were analysed by 2-DE. There was significant enrichment of specific proteins to both the hydrophobic or hydrophilic fractions. Some of the enriched hydrophobic proteins which discriminated the Helicobacter species were identified. The Helicobacter species that colonise at different sites in the gastrointestinal tract are exposed to different acidic environments. The ability of the bacteria to survive the different levels of acid stress may contribute towards the observed proteomic variation. Quantitative differences in protein abundance were demonstrated between bacteria grown under neutral and acidic conditions. The differential patterns of protein synthesis were most clearly detected when the sub-cellular hydrophobic and hydrophilic fractions were analysed by 2-DE.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:577627 |
| Date | January 2013 |
| Creators | Fowsantear, Winita |
| Publisher | University of Aberdeen |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Source | http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=201662 |
Page generated in 0.0021 seconds