The phosphate transport system of enteropathogenic Escherichia coli is involved in adherence to the host.

Evaluation of: Ferreira GM, Spira B: The pst operon of enteropathogenic Escherichia coli enhances bacterial adherence to epithelial cells. Microbiology 154(7), 2025-2036 (2008). Enteropathogenic Escherichia coli (EPEC) colonization of the human intestinal epithelium constitutes a complex, two-stage process, which involves multiple virulence factors that are expressed in response to numerous environmental signals.

The bundlin pilin protein of enteropathogenic Escherichia coli is an N-acetyllactosamine-specific lectin.

Synthetic N-acetyllactosamine (LacNAc) glycoside sequences coupled to BSA competitively inhibit enteropathogenic Escherichia coli (EPEC) localized adherence (LA) to human intestinal biopsy specimens and tissue culture cell monolayers. The LacNAc-specific adhesin appears to be associated with the bundle-forming pili (BFP) expressed by EPEC during the early stages of colonization. Herein, we report that recombinant bundlin inhibits EPEC LA to HEp-2 cells and binds to HEp-2 cells.

N-acetyllactosamine conjugated to gold nanoparticles inhibits enteropathogenic Escherichia coli colonization of the epithelium in human intestinal biopsy specimens.

We previously reported that the bundle-forming pilus-mediated localized adherence of enteropathogenic Escherichia coli to HEp-2, T84, and Caco-2 cells is inhibited by N-acetyllactosamine neoglycoconjugates. The results presented here extend this observation to the epithelium of biopsy specimens obtained from the human adult duodenum, terminal ileum, and colon.

Basis for N-acetyllactosamine-mediated inhibition of enteropathogenic Escherichia coli localized adherence.

In a previous article, the authors reported that exposing wild-type enteropathogenic Escherichia coli (EPEC) to chemically synthesized N-acetyllactosamine glycosides covalently coupled to BSA (LacNAc-BSA) inhibited localized adherence (LA) by these organisms and also caused them to lose their bundle-forming pili (BFP), the filamentous surface appendages responsible for their LA phenotype. This effect has now been further investigated by screening a panel of LacNAc-BSA-related glycosides for their ability to inhibit EPEC LA, which revealed that LacNAc-BSA retained its status as the most effective inhibitor of EPEC LA. It was also shown that LacNAc-BSA did not cause the loss of BFP in an EPEC strain containing a non-polar mutation in the bfpF gene and, as a consequence, unable to retract its BFP.