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The attachment of  Escherichia coli  O157:H7 to intestinal epithelial cells is indispensable for its pathogenesis. Besides translocated-intimin receptor (Tir),  E. coli  O157:H7 interacts with host cell surface receptors to promote intimate adhesion. This study showed that integrin β1 was increased in Caco-2 cells upon  E. coli  O157:H7 infection, while Caco-2 cells subjected to integrin β1 antibody blocking or CRISPR/Cas9 knockout had reduced bacterial attachment. Infection of  E. coli  O157:H7 inactivated focal adhesion kinase (FAK) and paxillin, increased focal adhesion (FA) and actin polymerization, and decreased cell migration in Caco-2 cells, which were rescued by integrin β1 antibody blocking or knockout. Pre-treatment with quercetin, known for its anti-oxidant and anti-inflammatory activity, reduced bacterial infection to Caco-2 cells, which might be partially via interfering integrin β1 and FAK association augmented by  E. coli  O157:H7. In addition, quercetin decreased FA formation induced by bacterial infection and recovered host cell motility. Taken together, data showed that  E. coli  O157:H7 interacts with integrin β1 to facilitate its adhesion to host cells. Quercetin inhibits bacterial infection possibly by blocking the interaction between  E. coli  O157:H7 and integrin β1. Collectively, these data indicate that quercetin provides an alternative antimicrobial to mitigate and control  E. coli  O157:H7 intestinal infection, and suggest potential broad benefits of quercetin and related polyphenols in fighting other enteric pathogen infections.

Quercetin Prevents Escherichia coli O157:H7 Adhesion to Epithelial Cells via Suppressing Focal Adhesions