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 (MAMHS), which contains an array of seven mammalian cell entry domains. The MAMHS 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 a physical barrier, and the barrier effect was enhanced by specific interactions between mucin and MAMHS in a sulfation-dependent manner. Desulfation of mucin by pure sulfatase or the sulfatase-producing commensal Bacteroides thetaiotaomicron decreased binding of E. coli to mucin and increased the attachment of bacteria to the epithelial surface via interactions with surface-localized sulfated lipid and protein receptors. Together, our results demonstrate that the E. coli adhesin MAMHS facilitates retention of a gut commensal by attachment to mucin. They further suggest that the amount of sulfatase secreted by mucin-foraging bacteria such as B. thetaiotaomicron, inhabiting the same niche, may affect the capacity of the mucus barrier to retain commensal E. coli.

Interactions between metabolically active bacteria and host gene expression at the cecal mucosa in pigs of diverging feed efficiency

“…Changes in cecal mucosal MUC2 expression may further explain the lower abundance of mucin-adherent Escherichia/Shigella in LRFI compared to HRFI pigs. The 3-O-sulfo-galactosyl moiety on host mucin acts as one of the prime adherence targets for the gut commensal E. coli (Al-Saedi et al, 2017). In this regard, relevance networking indicated the dependency of other low abundant mucosal bacteria (Blautia, Oscillospira, and Bacteroides) on mucosal MUC2 expression.…”

Defective phagocyte association during infection of Galleria mellonella with Yersinia pseudotuberculosis is detrimental to both insect host and microbe

“…Unlike other Yersinia adhesins (e.g. YadA, invasin, Ail), MAM homologs are present in a wide range of Gram-negative bacteria, although their ligand-binding specificities vary between species [ 3 , 8 , 9 ].…”

The anti-diarrhea activity of red algae-originated sulphated polysaccharides on ETEC-K88 infected mice

“…This toxin binds to sulphatide (3 0 -sulphogalactosyl-ceramide) receptors containing regions distributed on the intestinal epithelium cell wall. 39 Inhibition of STbP binding to its receptor was achieved by type l-carrageenan, a polymer extracted from seaweed and consisting of sulphated galactose units. 40 It is speculated that PHSP (hp) and GLSP (hp) could alleviate diarrhea by mimicking this toxin to compete with the receptor.…”