Adherence of Salmonella typhimurium to Caco-2 cells: identification of a glycoconjugate receptor.

The mechanism by which Salmonella species adhere to the epithelium of the intestine is not well understood. To identify components on intestinal epithelial cells that may be involved in the initial adherence of Salmonella typhimurium, we correlated patterns of adherence to well-differentiated Caco-2BBe cell monolayers with expression of brush border membrane components and lectin binding sites. This cloned cell line shows heterogeneous expression of sucrase-isomaltase and most lectin receptors. S. typhimurium adhered to a subpopulation of living or formaldehyde-fixed cells with a high multiplicity (up to 150 bacteria per cell). Bacterial binding to selected cells was not correlated with expression of the brush border hydrolases dipeptidyl-peptidase IV and sucrase-isomaltase or with binding of 10 of the 12 lectins tested. However, binding was correlated with the presence of binding sites for peanut agglutinin (PNA) [specific for Gal beta (1-3) GalNAc] and soybean agglutinin (specific for terminal GalNAc). Preincubation of live and fixed Caco-2BBe monolayers with PNA inhibited bacterial binding, while preincubation with soybean agglutinin did not. Electron microscopic analysis demonstrated that the initial adherence of S. typhimurium to Caco-2 cells in vitro involved peripheral components of the glycocalyx on apical microvilli. These results suggest that a Gal beta (1-3)GalNAc epitope recognized by PNA and located in the glycocalyx is involved in the early recognition events between S. typhimurium and Caco-2 cells and that differences in glycosylation patterns among individual epithelial cells may be a determinant in cell-selective adherence of S. typhimurium.