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Helicobacter spp. interactions with mucins: adhesion and mucin regulation of pathogen proliferation and gene expression

Författare Emma C Skoog
Datum för examination 2014-02-28
Opponent at public defense Dr. Marguerite Clyne, School of Medicine & Medical Science, Health Sciences Centre, Belfield, Dublin, Ireland
ISBN 978-91-628-8872-5
Förlag University of Gothenburg
Förlagsort Göteborg
Publiceringsår 2014
Publicerad vid Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Språk en
Länkar hdl.handle.net/2077/34818
Ämnesord Helicobacter, mucin, glycosylation, Lactobacillus, adhesion, proliferation, gene expression, CagA, SabA, BabA, ArsS, Fur
Ämneskategorier Medicinsk mikrobiologi, Medicinsk cellbiologi, Immunbiologi


Helicobacter pylori colonizes the gastric mucosa of approximately half of the world’s population and is a risk factor for gastritis, peptic ulcers and gastric cancer. H. pylori is surrounded by, and adheres to, the heavily glycosylated mucins that build up the mucus layer. The carbohydrate structures on the mucins that act as ligands for H. pylori vary between individuals and change during disease. In this thesis, we investigated how H. pylori interacts with differently glycosylated mucins by analyzing adhesion, proliferation, gene expression and the resulting effect on virulence to host cells. We found that mucins can interfere with H. pylori proliferation, partly dependent on binding to the mucins and the presence of known antimicrobial structures, but also observed an inhibition of H. pylori proliferation independent of these two factors. The gene expression of H. pylori varied greatly in the response to differently glycosylated mucins. Expression of the virulence factor CagA increased in response to some mucins, presumably by Fur-dependent regulation as a result of binding via the SabA adhesin. The varying interaction of H. pylori and mucins resulted in alterations in the response of infected gastric epithelial cells in vitro. There are several Helicobacter species that commonly infects other animals, but can also infect and cause disease in humans. Their modes of interaction with mucins are unclear. We examined the adhesion of two non-H. pylori Helicobacter species to differently glycosylated gastric mucins and mucosal tissue from a range of animals. Our results demonstrated that they can adhere to mucins and gastric tissue via specific glycan structures that change during infection, although the binding ability to human mucins are lower than that of H. pylori. In addition, there are other bacteria in the stomach that may interfere with mucin interactions of Helicobacter spp. We showed that Lactobacillus species isolated from the same stomachs as H. pylori did not compete for the same mucin ligands and did not markedly change how co-isolated H. pylori interact with the mucins. In summary, H. pylori adhesion to human mucins differs from that of other Helicobacter spp. and is not affected by co-colonizing Lactobacillus spp. The interactions of H. pylori to mucins affect proliferation and expression of virulence factors that may influence the colonization ability, virulence and host response and ultimately play a role in the development of symptoms displayed in the host.

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