Interactions of H. pylori with mucin. H. pylori chemotactically moves from a region of low concentration of mucin to a higher concentration and then binds to it. There may be competition between Nap binding to mucin (left pathway) and LPS interacting with the host mucin receptor, which would block the ability of mucin to bind its own receptor (right pathway). H. pylori mucinase activity degrades mucin either by removing sulfate residues (desulfation) or by cleaving the proteinaceous component of mucin (proteolysis). This allows H. pylori access to receptors on the host cell, leading to tighter adherence. Following adherence, mucin-containing granules are depleted, so that mucin release is perturbed. This leads to decreased mucin concentration in the mucous layer and would allow additional H. pylori to bind to gastric epithelial cells. There are very likely other H. pylori adhesins that interact with mucin, since mucin has a diverse repertoire of glycoconjugate moieties.