Immunolocalization of Hsc70 at Bacterially‐Generated Actin‐Rich Structures

Abstract

The actin cytoskeleton is commonly hijacked by bacterial pathogens. Listeria commandeers this filament system during their internalization, and for actin‐rich comet tail formation that enable the microbes to move within the infected cells as well as transfer from cell to cell. Enteropathogenic Escherichia coli (EPEC), an extracellular microbe, controls this cytoskeletal system when they generate E. coli pedestals as part of their firm docking to the plasma membrane of their host's cells and as they “surf” atop the infected cells. Finally, Salmonella exploit the host actin cytoskeleton to enter eukaryotic cells by forcing the generation of actin‐based membrane ruffling. We recently identified Hsc70 in a proteomics screen of EPEC pedestal components. This protein is normally involved with chaperoning functions within the cell. Despite there being a lack of evidence for an association of Hsc70 and actin, due to our proteomics identification of Hsc70 at EPEC pedestals we hypothesized that Hsc70 could be a common target of bacterial pathogens that control the actin cytoskeleton during their disease processes. To test this hypothesis we immunolocalized Hsc70 during Listeria, EPEC and Salmonella infections and found it concentrated at all actin structures generated by the microbes, demonstrating that this protein is a universal component for bacterial actin‐based structures.Support or Funding InformationFunding provided through NSERC. (Grant No. 355316 to J. A. G.)This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.