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Binding of Helicobacter pylori to Human Gastric Mucins Correlates with Binding of TFF1.

Ciara DunneJulie NaughtonGina DugganCatherine LoughreyMichelle KilcoyneLokesh JoshiStephen CarringtonHelen EarleySteffen BackertCatherine Robbe MasselotFelicity E B MayMarguerite Clyne
Published in: Microorganisms (2018)
Helicobacter pylori binds to the gastric mucin, MUC5AC, and to trefoil factor, TFF1, which has been shown to interact with gastric mucin. We examined the interactions of TFF1 and H. pylori with purified gastrointestinal mucins from different animal species and from humans printed on a microarray platform to investigate whether TFF1 may play a role in locating H. pylori in gastric mucus. TFF1 bound almost exclusively to human gastric mucins and did not interact with human colonic mucins. There was a strong correlation between binding of TFF1 and H. pylori to human gastric mucins, and between binding of both TFF1 and H. pylori to gastric mucins with that of Griffonia simplicifolia lectin-II, which is specific for terminal non-reducing α- or β-linked N-acetyl-d-glucosamine. These results suggest that TFF1 may help to locate H. pylori in a discrete layer of gastric mucus and hence restrain their interactions with epithelial cells.
Keyphrases
  • helicobacter pylori
  • endothelial cells
  • induced pluripotent stem cells
  • helicobacter pylori infection
  • pluripotent stem cells
  • dna binding