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Hsc70 is a Component of Bacterially Generated Actin-Rich Structures: An Immunolocalization Study
Brittany D Walker1, Michael D Chua1, Julian A Guttman1
1Department of Biological Sciences, Centre for Cell Biology, Development, and Disease (C2D2), Simon Fraser University, Burnaby, British Columbia, Canada.
Anatomical Record (Hoboken, N.J. : 2007)
|October 13, 2018
Summary
Heat shock cognate 70 protein (Hsc70) is recruited to actin structures during infections by enteropathogenic Escherichia coli (EPEC), Listeria, and Salmonella. This protein plays a role in bacterial pathogen interactions with host cells.
Area of Science:
- Microbiology
- Cell Biology
- Molecular Biology
Background:
- Enteropathogenic bacteria like EPEC, Salmonella typhimurium, and Listeria monocytogenes manipulate the host cell's actin cytoskeleton for invasion and intracellular transport.
- Previous research identified heat shock cognate 70 protein (Hsc70) as a potential component involved in actin pedestal formation during EPEC infections.
Purpose of the Study:
- To investigate the role of Hsc70 in the actin cytoskeleton rearrangements induced by various pathogenic bacteria.
- To determine if Hsc70 is specifically recruited to bacterial-induced actin structures.
Main Methods:
- Immunofluorescence microscopy was used to visualize the localization of Hsc70 and clathrin in cells infected with EPEC, Salmonella, and Listeria.
- Analysis focused on actin-rich structures formed during bacterial infections.
Main Results:
- Hsc70 was found to be recruited to actin-rich structures generated by EPEC, Salmonella, and Listeria.
- Hsc70 did not localize to the same cellular compartments as clathrin during these infections.
Conclusions:
- Hsc70 is a host protein recruited to bacterial-induced actin structures during infections by multiple enteropathogens.
- Hsc70's recruitment to these structures suggests a role in bacterial pathogenesis beyond its known functions in protein folding and clathrin uncoating.
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