Abstract
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.
Highlights
Helicobacter pylori is one of the most common infections of mankind, as half of the human world population carries the bacterium
Given the strict host specificity of H. pylori and its tropism for the gastric mucin, MUC5AC, and in light of our previous finding that H. pylori binds to TFF1 [13], we examined the interaction of TFF1 with human and animal mucins to investigate whether TFF1 might play a role in facilitating H. pylori colonization of gastric mucus
TFF1 is co-expressed with the gastric mucin MUC5AC by mucus secretory cells of the gastric mucosa [14]
Summary
Helicobacter pylori is one of the most common infections of mankind, as half of the human world population carries the bacterium. Given the strict host specificity of H. pylori and its tropism for the gastric mucin, MUC5AC, and in light of our previous finding that H. pylori binds to TFF1 [13], we examined the interaction of TFF1 with human and animal mucins to investigate whether TFF1 might play a role in facilitating H. pylori colonization of gastric mucus. Our results show that TFF1 binds exclusively to gastric mucins and there is a direct correlation between binding of H. pylori and binding of TFF1 to gastric mucins These results suggest that TFF1 may play a role in retaining the majority of H. pylori organisms in a specific stratum of gastric mucus rather than at the epithelial cell surface, which would limit inflammation and promote chronic infection
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