Calponins Are Recruited to Actin‐Rich Structures Generated by Pathogenic Escherichia coli , Listeria , and Salmonella
| Autor: | Jian Ping Jin, Michael Dominic Chua, Brittany Dominique Walker, Julian A. Guttman |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Histology Calponin macromolecular substances medicine.disease_cause Microbiology Enteropathogenic Escherichia coli 03 medical and health sciences Listeria monocytogenes medicine Humans Ecology Evolution Behavior and Systematics Actin Host cell membrane biology Chemistry Calcium-Binding Proteins Cell Membrane Microfilament Proteins Salmonella enterica musculoskeletal system biology.organism_classification Actins Calponin 1 Calponin 2 030104 developmental biology biology.protein Caco-2 Cells Anatomy Biotechnology |
| Zdroj: | The Anatomical Record. 301:2103-2111 |
| ISSN: | 1932-8494 1932-8486 |
| DOI: | 10.1002/ar.23956 |
| Popis: | The ingestion of enteropathogenic Escherichia coli (EPEC), Listeria monocytogenes, or Salmonella enterica serovar Typhimurium leads to their colonization of the intestinal lumen, which ultimately causes an array of ailments ranging from diarrhea to bacteremia. Once in the intestines, these microbes generate various actin-rich structures to attach, invade, or move within the host intestinal epithelial cells. Although an assortment of actin-associated proteins has been identified to varying degrees at these structures, the localization of many actin stabilizing proteins have yet to be analyzed. Here, we examined the recruitment of the actin-associated proteins, calponin 1 and 2 at EPEC pedestals, L. monocytogenes actin clouds, comet tails and listeriopods, and S. Typhimurium membrane ruffles. In other systems, calponins are known to bind to and stabilize actin filaments. In EPEC pedestals, calponin 1 was recruited uniformly throughout the structures while calponin 2 was enriched at the apical tip. During L. monocytogenes infections, calponin 1 was found through all the actin-rich structures generated by the bacteria, while calponin 2 was only present within actin-rich structures formed by L. monocytogenes near the host cell membrane. Finally, both calponins were found within S. Typhimurium-generated membrane ruffles. Taken together, we have shown that although calponin 1 is recruited to actin-rich structures formed by the three bacteria, calponin 2 is specifically recruited to only membrane-bound actin-rich structures formed by the bacteria. Thus, our findings suggest that calponin 2 is a novel marker for membrane-bound actin structures formed by pathogenic bacteria. Anat Rec, 301:2103-2111, 2018. © 2018 Wiley Periodicals, Inc. |
| Databáze: | OpenAIRE |
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