Functional analysis of Escherichia coli Yad fimbriae reveals their potential role in environmental persistence.

Initial adhesion of bacterial cells to surfaces or host tissues is a key step in colonisation and biofilm formation processes, and is mediated by cell surface appendages. It was previously demonstrated that Escherichia coli K-12 possesses an arsenal of silenced chaperone-usher fimbriae that were functional when constitutively expressed. Among them, production of prevalent Yad fimbriae induces adhesion to abiotic surfaces. Functional characterisation of Yad fimbriae were undertook, and YadN was identified as the most abundant and potential major pilin, and YadC as the potential tip-protein of Yad fimbriae. It was showed that Yad production participates to binding of E. coli K-12 to human eukaryotic cells (Caco-2) and inhibits macrophage phagocytosis, but also enhances E. coli K-12 binding to xylose, a major component of the plant cell wall, through its tip-lectin YadC. Consistently, it was demonstrated that Yad production provides E. coli with a competitive advantage in colonising corn seed rhizospheres. The latter phenotype is correlated with induction of Yad expression at temperatures below 37°C, and under anaerobic conditions, through a complex regulatory network. Taken together, these results suggest that Yad fimbriae are versatile adhesins that beyond potential capacities to modulate host-pathogen interactions might contribute to E. coli environmental persistence.

Inhibition of type 1 fimbriae-mediated Escherichia coli adhesion and biofilm formation by trimeric cluster thiomannosides conjugated to diamond nanoparticles.

Recent advances in nanotechnology have seen the development of a number of microbiocidal and/or anti-adhesive nanoparticles displaying activity against biofilms. In this work, trimeric thiomannoside clusters conjugated to nanodiamond particles (ND) were targeted for investigation. NDs have attracted attention as a biocompatible nanomaterial and we were curious to see whether the high mannose glycotope density obtained upon grouping monosaccharide units in triads might lead to the corresponding ND-conjugates behaving as effective inhibitors of E. coli type 1 fimbriae-mediated adhesion as well as of biofilm formation. The required trimeric thiosugar clusters were obtained through a convenient thiol-ene "click" strategy and were subsequently conjugated to alkynyl-functionalized NDs using a Cu(I)-catalysed "click" reaction. We demonstrated that the tri-thiomannoside cluster-conjugated NDs (ND-Man3) show potent inhibition of type 1 fimbriae-mediated E. coli adhesion to yeast and T24 bladder cells as well as of biofilm formation. The biofilm disrupting effects demonstrated here have only rarely been reported in the past for analogues featuring such simple glycosidic motifs. Moreover, the finding that the tri-thiomannoside cluster (Man3N3) is itself a relatively efficient inhibitor, even when not conjugated to any ND edifice, suggests that alternative mono- or multivalent sugar-derived analogues might also be usefully explored for E. coli-mediated biofilm disrupting properties.