The Serine Protease EspC from Enteropathogenic Regulates Pore Formation and Cytotoxicity Mediated by the Type III Secretion System

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Enteropathogenic Escherichia coli (EPEC) is an important diarrheal pathogen responsible for infant diarrhoea associated with significant morbidity and mortality rates in developing countries. Upon ingestion EPEC colonizes the intestinal mucosa, causing characteristic lesions on enterocytes. Using a type III secretion system (T3SS) acting as a molecular syringe, EPEC injects numerous bacterial proteins into host cells that disrupt the intestinal epithelium homeostasis. Injection of T3SS proteins requires the insertion into the host cell plasma membrane of bacterial protein complex, called the "translocon", associated with pore-forming activity. In addition to the T3SS, EPEC also secretes other bacterial toxins involved in virulence. Among these, the EspC is a protease reported to degrade various host proteins. In this paper, we have characterized an "unsuspected role" for EspC. We show that EspC degrades the T3SS translocon components following cell contact and regulates T3SS-dependent pore formation in epithelial cells. The EspC control of pore formation limits cytotoxicity and thus, is expected to limit the emission of danger signals, which would otherwise favour bacterial clearance at the onset of infection. This work describes a novel regulatory mechanism of pore formation mediated by the T3SS, that are likely to be relevant for other extracellular pathogens.

Vyšlo v časopise: The Serine Protease EspC from Enteropathogenic Regulates Pore Formation and Cytotoxicity Mediated by the Type III Secretion System. PLoS Pathog 11(7): e32767. doi:10.1371/journal.ppat.1005013
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1005013

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