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Escherichia coli  O157:H7 is the most well-studied serotype of the enterohemorrhagic  E .  coli  (EHEC) class of  E .  coli  intestinal pathogens and is responsible for many outbreaks of serious food-borne illness worldwide each year. Adherence mechanisms are a critical component of its pathogenesis, persistence in natural reservoirs, and environmental contamination.  E .  coli  O157:H7 has a highly effective virulence operon, the Locus of Enterocyte Effacement (LEE), and its encoded intimate adherence mechanism is well characterized. However, factors involved in the preceding initial attachment are not well understood. In this study, we propose a mechanism of initial adherence used by  E .  coli  O157:H7  in vitro . We describe a bacterial protein not previously reported to be involved in adherence, Slp, and its interactions with the human host protein polymeric immunoglobulin receptor (pIgR). The human pIgR has previously been shown to act as an adherence receptor for some mucosal pathogens and is highly expressed in the intestine. Following observation of significant colocalization between  E .  coli  O157:H7 bacteria and pIgR location on Caco-2 cells, a co-immunoprecipitation (Co-IP) assay using a human recombinant Fc-tagged pIgR protein led to the identification of this protein. Disruption of Slp expression in  E .  coli  O157:H7, through deletion of its encoding gene  slp , produced a significant adherence deficiency to Caco-2 cells at early time points associated with initial adherence. Plasmid complementation of the  slp  gene fully restored the wild-type phenotype. Furthermore, immunofluorescence microscopy revealed evidence that this interaction is specific to the pathogenic strains of  E .  coli  tested and not the nonpathogenic control strain  E .  coli  K12. Additionally, deletion of  slp  gene resulted in the absence of the corresponding protein band in further Co-IP assays, while the plasmid-encoded  slp  gene complementation of the deletion mutant strain restored the wild-type pattern. These data support the proposal that Slp directly contributes to initial adherence, with the pIgR protein as its proposed receptor.

plos one

The Escherichia coli O157:H7 carbon starvation-inducible lipoprotein Slp contributes to initial adherence in vitro via the human polymeric immunoglobulin receptor