Overexpressed Palladin Rescues Enteropathogenic E. coli (EPEC) Pedestal Lengths in ArpC2 Depleted Cells.

Abstract

Enteropathogenic Escherichia coli (EPEC) causes diarrheal disease. Once ingested, these extracellular pathogens attach to the intestinal epithelial cells of their host, collapse the localized microvilli, and generate actin-rich structures within the host cells that are located beneath the attached bacteria, called "pedestals." Palladin is an actin-associated protein that cross-links and stabilizes actin filaments. This protein also acts as a scaffolding protein for other actin-binding proteins. Here, we examine the role of Palladin during EPEC infections and show that Palladin is co-opted by EPEC. Depletion of Palladin resulted in shorter pedestals, and when Palladin containing mutations in either its actin- or VASP-binding domains were overexpressed in cells, pedestals decreased in length. Importantly, we show that the overexpression of Palladin in ArpC2^-/- (Arp2/3 complex-depleted) cells rescued pedestal length. Together, our results demonstrate that Palladin has the ability to rescue pedestal length during EPEC infections when the function of the Arp2/3 complex is diminished.