3-Sulfogalactosyl-dependent adhesion of Escherichia coli HS multivalent adhesion molecule is attenuated by sulfatase activity.

ABSTRACT: Bacterial adhesion to host receptors is an early and essential step in bacterial colonization, and the nature of adhesin-receptor interactions determines bacterial localization and thus the outcome of these interactions. Here, we determined the host receptors for the multivalent adhesion molecule (MAM) from the gut commensal Escherichia coli HS (MAM^HS), which contains an array of seven mammalian cell entry domains. The MAM^HS adhesin interacted with a range of host receptors, through recognition of a shared 3-O-sulfogalactosyl moiety. This functional group is also found in mucin, a component of the intestinal mucus layer and thus one of the prime adherence targets for commensal E. coli Mucin gels impeded the motility of E. coli by acting as

SUBMITTER: Al-Saedi F 

PROVIDER: S-EPMC5712619 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature